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Volumn 72, Issue 5, 1997, Pages 1963-1985

The transmembrane 7-α-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN;

EID: 0030998038     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(97)78842-8     Document Type: Article
Times cited : (143)

References (152)
  • 1
    • 0029818551 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: A site-directed spin-labeling study
    • Altenbach, C., K. Yang, D. L. Farrens, Z. T. Farahbakhsh, H. G. Khorana, and W. L. Hubbell. 1996. Structural features and light-dependent changes in the cytoplasmic interhelical E-F loop region of rhodopsin: a site-directed spin-labeling study. Biochemistry. 35:12470-12478.
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1    Yang, K.2    Farrens, D.L.3    Farahbakhsh, Z.T.4    Khorana, H.G.5    Hubbell, W.L.6
  • 2
    • 0023660022 scopus 로고
    • Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus
    • Altschuh, D., A. M. Lesk, A. C. Bloomer, and A. Klug. 1987. Correlation of co-ordinated amino acid substitutions with function in viruses related to tobacco mosaic virus. J. Mol. Biol. 193:693-707.
    • (1987) J. Mol. Biol. , vol.193 , pp. 693-707
    • Altschuh, D.1    Lesk, A.M.2    Bloomer, A.C.3    Klug, A.4
  • 3
    • 0028061193 scopus 로고
    • A conservative carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Amis, S., K. Fahmy, K. P. Hofmann, and T. P. Sakmar. 1994. A conservative carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin, J. Biol. Chem. 269:23879-23881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Amis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 4
    • 0024803054 scopus 로고
    • A study of the binding site requirements of rhodopsin using isomers of alpha-retinal and 5-substituted alpha-retinal analogs
    • Asato, A. E., B.-W. Zhang, M. Denny, T. Mirzadegan, K. Seff, and R. S. H. Liu. 1989. A study of the binding site requirements of rhodopsin using isomers of alpha-retinal and 5-substituted alpha-retinal analogs. Bioorg. Khim. 17:410-421.
    • (1989) Bioorg. Khim. , vol.17 , pp. 410-421
    • Asato, A.E.1    Zhang, B.-W.2    Denny, M.3    Mirzadegan, T.4    Seff, K.5    Liu, R.S.H.6
  • 5
    • 0028289475 scopus 로고
    • Molecular determinants of human red/green color discrimination
    • Asenjo, A. B., J. Rim, and D. D. Oprian. 1994. Molecular determinants of human red/green color discrimination. Neuron. 12:1131-1138.
    • (1994) Neuron. , vol.12 , pp. 1131-1138
    • Asenjo, A.B.1    Rim, J.2    Oprian, D.D.3
  • 8
    • 0027506471 scopus 로고
    • The probable arrangement of the helices in G protein-coupled receptors
    • Baldwin, J. M. 1993. The probable arrangement of the helices in G protein-coupled receptors. EMBO J. 12:1693-1703.
    • (1993) EMBO J. , vol.12 , pp. 1693-1703
    • Baldwin, J.M.1
  • 9
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G proteins
    • Baldwin, J. M. 1994. Structure and function of receptors coupled to G proteins. Curr. Opin. Cell Biol. 6:180-190.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 11
    • 0021763375 scopus 로고
    • Labelling of the cytoplasmic domains of ovine rhodopsin with hydrophilic chemical probes
    • Barclay, P. L. and J. B. C. Findlay. 1984. Labelling of the cytoplasmic domains of ovine rhodopsin with hydrophilic chemical probes. Biochem. J. 220:75-84.
    • (1984) Biochem. J. , vol.220 , pp. 75-84
    • Barclay, P.L.1    Findlay, J.B.C.2
  • 12
    • 0024278714 scopus 로고
    • Helix geometry in proteins
    • Barlow, D. J. and J. M. Thornton. 1988. Helix geometry in proteins. J. Mol. Biol. 201:601-619.
    • (1988) J. Mol. Biol. , vol.201 , pp. 601-619
    • Barlow, D.J.1    Thornton, J.M.2
  • 14
    • 0028178528 scopus 로고
    • Determination of α-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme
    • Blaber, M., X.-J. Zhang, J. D. Lindstrom, S. D. Pepiot, W. A. Baase, and B. W. Matthews. 1994. Determination of α-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J. Mol. Biol. 235:600-624.
    • (1994) J. Mol. Biol. , vol.235 , pp. 600-624
    • Blaber, M.1    Zhang, X.-J.2    Lindstrom, J.D.3    Pepiot, S.D.4    Baase, W.A.5    Matthews, B.W.6
  • 15
    • 0028233906 scopus 로고
    • Insertional mutagenesis as a probe of rhodopsin's topography, stability, and activity
    • Borjigin, J. and J. Nathans. 1994. Insertional mutagenesis as a probe of rhodopsin's topography, stability, and activity. J. Biol. Chem. 269: 14715-14722.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14715-14722
    • Borjigin, J.1    Nathans, J.2
  • 17
    • 0017226063 scopus 로고
    • Molecular flow resonance Raman effect from retinal and rhodopsin
    • Callender, R. H., A. Doukas, R. Crouch, and K. Nakanishi. 1976. Molecular flow resonance Raman effect from retinal and rhodopsin. Biochemistry. 15:1621-1629.
    • (1976) Biochemistry , vol.15 , pp. 1621-1629
    • Callender, R.H.1    Doukas, A.2    Crouch, R.3    Nakanishi, K.4
  • 18
    • 0027986462 scopus 로고
    • Mutation of an aspartate residue highly conserved among G-protein-coupled receptors results in nonreciprocal disruption of alpha-2-adrenergic receptor-G-protein interactions. A negative charge at amino acid residue. 79 forecasts alpha-2A-adrenergic receptor sensitivity to allosteric modulation by monovalent cations and fully effective receptor/G-protein coupling
    • Ceresa, B. P. and L. E. Limbird. 1994. Mutation of an aspartate residue highly conserved among G-protein-coupled receptors results in nonreciprocal disruption of alpha-2-adrenergic receptor-G-protein interactions. A negative charge at amino acid residue. 79 forecasts alpha-2A-adrenergic receptor sensitivity to allosteric modulation by monovalent cations and fully effective receptor/G-protein coupling. J. Biol. Chem. 269:29557-29564.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29557-29564
    • Ceresa, B.P.1    Limbird, L.E.2
  • 19
    • 0018507365 scopus 로고
    • Orientation of aromatic residues in rhodopsin. Rotation of one tryptophan upon the Meta I to Meta II transition after illumination
    • Chabre, M., and J. Breton. 1979a. Orientation of aromatic residues in rhodopsin. Rotation of one tryptophan upon the Meta I to Meta II transition after illumination. Photochem. Photobiol. 30:295-299.
    • (1979) Photochem. Photobiol. , vol.30 , pp. 295-299
    • Chabre, M.1    Breton, J.2
  • 20
    • 0018320164 scopus 로고
    • The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states, and the reversibility of the Meta II-Meta III transition
    • Chabre, M., and J. Breton. 1979b. The orientation of the chromophore of vertebrate rhodopsin in the "Meta" intermediate states, and the reversibility of the Meta II-Meta III transition. Vision Res. 19:1005-1018.
    • (1979) Vision Res. , vol.19 , pp. 1005-1018
    • Chabre, M.1    Breton, J.2
  • 21
    • 0026661975 scopus 로고
    • Introduction of hydroxyl-bearing amino acids causes bathochromic spectral shifts in rhodopsin. Amino acid substitutions responsible for red-green color pigment spectral tuning
    • Chan, T., M. Lee, and T. P. Sakmar. 1992. Introduction of hydroxyl-bearing amino acids causes bathochromic spectral shifts in rhodopsin. Amino acid substitutions responsible for red-green color pigment spectral tuning. J. Biol. Chem. 267:9478-9480.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9478-9480
    • Chan, T.1    Lee, M.2    Sakmar, T.P.3
  • 24
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., and A. M. Lesk. 1986. The relation between the divergence of sequence and structure in proteins. EMBO J. 5:823-826.
    • (1986) EMBO J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 25
    • 0028881209 scopus 로고
    • Disulfide mutants of bamase I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography
    • Clarke, J., K. Henrick, and A. R. Fersht. 1995. Disulfide mutants of bamase I: changes in stability and structure assessed by biophysical methods and X-ray crystallography. J. Mol. Biol. 253:493-504.
    • (1995) J. Mol. Biol. , vol.253 , pp. 493-504
    • Clarke, J.1    Henrick, K.2    Fersht, A.R.3
  • 26
    • 0027298812 scopus 로고
    • Constitutive activation of opsin: Influence of charge at position 134 and size at position 296
    • Cohen, G. B., T. Yang, P. R. Robinson, and D. D. Oprian. 1993. Constitutive activation of opsin: influence of charge at position 134 and size at position 296. Biochemistry. 32:6111-6115.
    • (1993) Biochemistry , vol.32 , pp. 6111-6115
    • Cohen, G.B.1    Yang, T.2    Robinson, P.R.3    Oprian, D.D.4
  • 28
    • 0022543490 scopus 로고
    • 125I]iodobenzene. Labelling of the chromophore-attachment domain
    • 125I]iodobenzene. Labelling of the chromophore-attachment domain. Biochem. J. 234: 413-420.
    • (1986) Biochem. J. , vol.234 , pp. 413-420
    • Davison, M.D.1    Findlay, J.B.C.2
  • 30
    • 0025790423 scopus 로고
    • Structures of bacterial photosynthetic reaction centers
    • Deisenhofer, J., and H. Michel. 1991. Structures of bacterial photosynthetic reaction centers. Annu. Rev. Cell Biol. 7:1-23.
    • (1991) Annu. Rev. Cell Biol. , vol.7 , pp. 1-23
    • Deisenhofer, J.1    Michel, H.2
  • 31
    • 0028266198 scopus 로고
    • Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: A resonance Raman study of the Schiff base hydrogen/deuterium exchange
    • Deng, H., L. Huang, R. Callender, and T. Ebrey. 1994. Evidence for a bound water molecule next to the retinal Schiff base in bacteriorhodopsin and rhodopsin: a resonance Raman study of the Schiff base hydrogen/deuterium exchange. Biophys. J. 66:1129-1136.
    • (1994) Biophys. J. , vol.66 , pp. 1129-1136
    • Deng, H.1    Huang, L.2    Callender, R.3    Ebrey, T.4
  • 32
    • 0023656534 scopus 로고
    • The multiple membrane spanning topography of the beta 2-adrenergic receptor. Localization of the sites of binding, glycosylation, and regulatory phosphorylation by limited proteolysis
    • Dohlman, H. G., M. Bouvier, J. L. Benovic, M. G. Caron, and R. J. Lefkowitz. 1987. The multiple membrane spanning topography of the beta 2-adrenergic receptor. Localization of the sites of binding, glycosylation, and regulatory phosphorylation by limited proteolysis. J. Biol. Chem. 262:14282-14288.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14282-14288
    • Dohlman, H.G.1    Bouvier, M.2    Benovic, J.L.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 33
    • 0027959026 scopus 로고
    • Seven-helix receptors: Structure and modelling
    • Donnelly, D., and J. B. C. Findlay. 1994. Seven-helix receptors: structure and modelling. Curr. Opin. Struct. Biol. 4:582-589.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 582-589
    • Donnelly, D.1    Findlay, J.B.C.2
  • 34
    • 0028235604 scopus 로고
    • The evolution and structure of aminergic G protein-coupled receptors
    • Donnelly, D., J. B. C. Findlay, and T. L. Blundell. 1994. The evolution and structure of aminergic G protein-coupled receptors. Receptors Channels. 2:61-78.
    • (1994) Receptors Channels , vol.2 , pp. 61-78
    • Donnelly, D.1    Findlay, J.B.C.2    Blundell, T.L.3
  • 35
    • 0027497369 scopus 로고
    • Modeling α-helical transmembrane domains: The calculation and use of subsitution tables for lipid-facing residues
    • Donnelly, D., J. P. Overington, S. V. Ruffle, J. H. A. Nugent, and T. L. Blundell. 1993. Modeling α-helical transmembrane domains: the calculation and use of subsitution tables for lipid-facing residues. Protein Sci. 2:55-70.
    • (1993) Protein Sci. , vol.2 , pp. 55-70
    • Donnelly, D.1    Overington, J.P.2    Ruffle, S.V.3    Nugent, J.H.A.4    Blundell, T.L.5
  • 36
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
    • Elling, C. E., S. M. Nielsen, and T. W. Schwartz. 1995. Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature. 374:74-77.
    • (1995) Nature , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 37
    • 0027374544 scopus 로고
    • Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin. II. A Fourier-transform infrared spectroscopy study of site-directed mutants
    • Fahmy, K., F. Jäger, M. Beck, T. A. Zvyaga, T. P. Sakmar, and F. Seibert. 1993. Protonation states of membrane-embedded carboxylic acid groups in rhodopsin and metarhodopsin. II. A Fourier-transform infrared spectroscopy study of site-directed mutants. Proc. Natl. Acad. Sci. USA. 90:10206-10210.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10206-10210
    • Fahmy, K.1    Jäger, F.2    Beck, M.3    Zvyaga, T.A.4    Sakmar, T.P.5    Seibert, F.6
  • 38
    • 0002843161 scopus 로고
    • Comparative molecular dynamics study of the seven-helix bundle arrangment of G-protein coupled receptors
    • Fanelli, F., M. C. Menziani, M. Cocchi, and P. G. De Benedetti. 1995a. Comparative molecular dynamics study of the seven-helix bundle arrangment of G-protein coupled receptors. J. Mol. Struct. (Theochem.). 333:49-69.
    • (1995) J. Mol. Struct. (Theochem.) , vol.333 , pp. 49-69
    • Fanelli, F.1    Menziani, M.C.2    Cocchi, M.3    De Benedetti, P.G.4
  • 40
    • 0027716597 scopus 로고
    • Photoactivated conformational changes in rhodopsin: A time resolved spin label study
    • Farahbakhsh, Z. T., K. Hideg, and W. L. Hubbell. 1993. Photoactivated conformational changes in rhodopsin: a time resolved spin label study. Science. 262:1416-1419.
    • (1993) Science , vol.262 , pp. 1416-1419
    • Farahbakhsh, Z.T.1    Hideg, K.2    Hubbell, W.L.3
  • 41
    • 0029035661 scopus 로고
    • Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: A site-directed spin labeling study
    • Farahbakhsh, Z. T., K. D. Ridge, H. G. Khorana, and W. L. Hubbell. 1995. Mapping light-dependent structural changes in the cytoplasmic loop connecting helices C and D in rhodopsin: a site-directed spin labeling study. Biochemistry. 34:8812-8819.
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1    Ridge, K.D.2    Khorana, H.G.3    Hubbell, W.L.4
  • 42
    • 0025284257 scopus 로고
    • The evolution of α/β barrel enzymes
    • Farber, G. K., and G. A. Petsko. 1990. The evolution of α/β barrel enzymes. Trends Biochem. Sci. 15:228-234.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 43
    • 0029670790 scopus 로고    scopus 로고
    • 583 in the third extracellular loop of the lutropin/choriogonadotropin receptor is critical for signaling
    • 583 in the third extracellular loop of the lutropin/choriogonadotropin receptor is critical for signaling. J. Biol. Chem. 271:925-930.
    • (1996) J. Biol. Chem. , vol.271 , pp. 925-930
    • Fernandez, L.M.1    Puett, D.2
  • 44
    • 0029964709 scopus 로고    scopus 로고
    • Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/ choriogonadotropin receptor involved in signaling
    • Fernandez, L. M., and D. Puett. 1996b. Identification of amino acid residues in transmembrane helices VI and VII of the lutropin/ choriogonadotropin receptor involved in signaling. Biochemistry. 35: 3986-3993.
    • (1996) Biochemistry , vol.35 , pp. 3986-3993
    • Fernandez, L.M.1    Puett, D.2
  • 45
    • 0024341576 scopus 로고
    • Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A Fourier transform infrared and biochemical investigation
    • Canter, U. M., E. D. Schmid, D. Perez-Sala, R. R. Rando, and F. Siebert. 1989. Removal of the 9-methyl group of retinal inhibits signal transduction in the visual process. A Fourier transform infrared and biochemical investigation. Biochemistry. 28:5954-5962.
    • (1989) Biochemistry , vol.28 , pp. 5954-5962
    • Canter, U.M.1    Schmid, E.D.2    Perez-Sala, D.3    Rando, R.R.4    Siebert, F.5
  • 46
    • 0026264506 scopus 로고
    • Quantum yield of CHAPSO-solubilized rhodopsin and 3-hydroxy retinal containing bovine opsin
    • Gärtner, W., D. Ullrich, and K. Vogt. 1991. Quantum yield of CHAPSO-solubilized rhodopsin and 3-hydroxy retinal containing bovine opsin. Photochem. Photobiol. 54:1047-1055.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 1047-1055
    • Gärtner, W.1    Ullrich, D.2    Vogt, K.3
  • 47
    • 0001478782 scopus 로고
    • The crystal and molecular structure of 11-cis-retinal
    • Gilardi, R. D., I. L. Karle, and J. Karle. 1972. The crystal and molecular structure of 11-cis-retinal. Acta Crystallogr. B28:2605-2612.
    • (1972) Acta Crystallogr. , vol.B28 , pp. 2605-2612
    • Gilardi, R.D.1    Karle, I.L.2    Karle, J.3
  • 48
    • 0025483161 scopus 로고
    • Optimization, constraint, and history in the evolution of eyes
    • Goldsmith, T. H. 1990. Optimization, constraint, and history in the evolution of eyes. Q. Rev. Biol. 65: 281-322.
    • (1990) Q. Rev. Biol. , vol.65 , pp. 281-322
    • Goldsmith, T.H.1
  • 49
  • 50
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structure in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., W. Brawn, and K. Wüthrich. 1991. Efficient computation of three-dimensional protein structure in solution from NMR data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Brawn, W.2    Wüthrich, K.3
  • 51
    • 0027199085 scopus 로고
    • Localization of the retinal protonated Schiff base counterion in rhodopsin
    • Han, M., B. S. DeDecker, and S. O. Smith. 1993. Localization of the retinal protonated Schiff base counterion in rhodopsin. Biophys. J. 65:899-906.
    • (1993) Biophys. J. , vol.65 , pp. 899-906
    • Han, M.1    DeDecker, B.S.2    Smith, S.O.3
  • 52
    • 0029730779 scopus 로고    scopus 로고
    • Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant
    • Han, M., S. W. Lin, M. Minkova, S. O. Smith, and T. P. Sakmar. 1996a. Functional interaction of transmembrane helices 3 and 6 in rhodopsin. Replacement of phenylalanine 261 by alanine causes reversion of phenotype of a glycine 121 replacement mutant. J. Biol. Chem. 271: 32337-32342.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32337-32342
    • Han, M.1    Lin, S.W.2    Minkova, M.3    Smith, S.O.4    Sakmar, T.P.5
  • 53
    • 0029753237 scopus 로고    scopus 로고
    • The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin
    • Han, M., S. W. Lin, S. O. Smith, and T. P. Sakmar. 1996b. The effects of amino acid replacements of glycine 121 on transmembrane helix 3 of rhodopsin. J. Biol. Chem. 271:32330-32336.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32330-32336
    • Han, M.1    Lin, S.W.2    Smith, S.O.3    Sakmar, T.P.4
  • 54
    • 0029116477 scopus 로고
    • High-resolution structural studies of the retinal-Glu113 intheraction in rhodopsin
    • Han, M., and S. O. Smith. 1995a. High-resolution structural studies of the retinal-Glu113 intheraction in rhodopsin. Biophys. Chem. 56:23-29.
    • (1995) Biophys. Chem. , vol.56 , pp. 23-29
    • Han, M.1    Smith, S.O.2
  • 55
    • 0028916739 scopus 로고
    • NMR constraints on the location of the retinal chromophore in rhodopsin and bathorodopsin
    • Han, M., and S. O. Smith. 1995b. NMR constraints on the location of the retinal chromophore in rhodopsin and bathorodopsin. Biochemistry. 34: 1425-1432.
    • (1995) Biochemistry , vol.34 , pp. 1425-1432
    • Han, M.1    Smith, S.O.2
  • 56
    • 0028238582 scopus 로고
    • Pattern recognition and self-correcting distance geometry calculations applied to myohemerythrin
    • Hänggi, G., and W. Braun. 1994. Pattern recognition and self-correcting distance geometry calculations applied to myohemerythrin. FEBS Lett. 334:147-153.
    • (1994) FEBS Lett. , vol.334 , pp. 147-153
    • Hänggi, G.1    Braun, W.2
  • 57
    • 0027425382 scopus 로고
    • Amino acid sequence surronding the retinal-binding site in retinochrome of the squid, Todarodes pacificus
    • Hara-Nishimura, I., M. Kondo, M. Nishimura, R. Hara, and T. Hara. 1993. Amino acid sequence surronding the retinal-binding site in retinochrome of the squid, Todarodes pacificus. FEBS Lett. 335:94-98.
    • (1993) FEBS Lett. , vol.335 , pp. 94-98
    • Hara-Nishimura, I.1    Kondo, M.2    Nishimura, M.3    Hara, R.4    Hara, T.5
  • 59
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., J. M. Baldwin, T. A. Ceska, F. Zemlin, E. Beckmann, and K. H. Downing. 1990. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213: 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 60
    • 0028829235 scopus 로고
    • Automated method for modeling seven-helix transmembrane receptors from experimental data
    • Herzyk, P., and R. E. Hubbard, 1995. Automated method for modeling seven-helix transmembrane receptors from experimental data. Biophys. J. 69:2419-2442.
    • (1995) Biophys. J. , vol.69 , pp. 2419-2442
    • Herzyk, P.1    Hubbard, R.E.2
  • 61
    • 0017171319 scopus 로고
    • Visual-pigment spectra: Implications of the protonation of the retinal Schiff base
    • Honig, B., A. D. Greenberg, U. Dinur, and T. G. Ebrey. 1976. Visual-pigment spectra: implications of the protonation of the retinal Schiff base. Biochemistry. 15:4593-4599.
    • (1976) Biochemistry , vol.15 , pp. 4593-4599
    • Honig, B.1    Greenberg, A.D.2    Dinur, U.3    Ebrey, T.G.4
  • 62
    • 0001909239 scopus 로고
    • Theoretical studies of the visual chromophore
    • Honig, B., A. Warsel, and M. Karplus. 1975. Theoretical studies of the visual chromophore. Accounts Chem. Res. 8:92-100.
    • (1975) Accounts Chem. Res. , vol.8 , pp. 92-100
    • Honig, B.1    Warsel, A.2    Karplus, M.3
  • 63
    • 0025642404 scopus 로고
    • An aspartate conserved among G-protein receptors confers allosteric regulation of alpha 2-adrenergic receptors by sodium
    • Horstman, D. A., S. Brandon, A. L. Wilson, C. A. Guyer, E. J. Cragoe, Jr., and L. E. Limbird. 1990. An aspartate conserved among G-protein receptors confers allosteric regulation of alpha 2-adrenergic receptors by sodium. J. Biol. Chem. 265:21590-21595.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21590-21595
    • Horstman, D.A.1    Brandon, S.2    Wilson, A.L.3    Guyer, C.A.4    Cragoe E.J., Jr.5    Limbird, L.E.6
  • 64
    • 0028962470 scopus 로고
    • Critical role of a conserved intramembrane tyrosine residue in angiotensin II receptor activation
    • Hunyady, L., M. Bor, T. Balla, and K. J. Catt. 1995. Critical role of a conserved intramembrane tyrosine residue in angiotensin II receptor activation. J. Biol. Chem. 270:9702-9705.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9702-9705
    • Hunyady, L.1    Bor, M.2    Balla, T.3    Catt, K.J.4
  • 65
    • 0014668709 scopus 로고
    • Effect of solvent polarizability on the absorption spectrum of all-trans-retinylpyrrolidiniminium perchlorate
    • Irving, C. S., G. W. Byers, and P. A. Leermakers. 1969. Effect of solvent polarizability on the absorption spectrum of all-trans-retinylpyrrolidiniminium perchlorate. J. Am. Chem. Soc. 91:2141-2143.
    • (1969) J. Am. Chem. Soc. , vol.91 , pp. 2141-2143
    • Irving, C.S.1    Byers, G.W.2    Leermakers, P.A.3
  • 66
    • 0028017506 scopus 로고
    • Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin
    • Jäger, F., K. Fahmy, T. P. Sakmar, and F. Siebert. 1994a. Identification of glutamic acid 113 as the Schiff base proton acceptor in the metarhodopsin II photointermediate of rhodopsin. Biochemistry. 33:10878-10882.
    • (1994) Biochemistry , vol.33 , pp. 10878-10882
    • Jäger, F.1    Fahmy, K.2    Sakmar, T.P.3    Siebert, F.4
  • 67
    • 0028179864 scopus 로고
    • Interactions of the β-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins
    • Jäger, F., S. Jäger, O. Krutle, N. Friedman, M. Sheves, K. P. Hofmann, and F. Siebert. 1994b. Interactions of the β-ionone ring with the protein in the visual pigment rhodopsin control the activation mechanism. An FTIR and fluorescence study on artificial vertebrate rhodopsins. Biochemistry. 33:7389-7397.
    • (1994) Biochemistry , vol.33 , pp. 7389-7397
    • Jäger, F.1    Jäger, S.2    Krutle, O.3    Friedman, N.4    Sheves, M.5    Hofmann, K.P.6    Siebert, F.7
  • 68
    • 0028211273 scopus 로고
    • A model recognition approach to the prediction of all-helical membrane protein structure and topology
    • Jones, D. T., W. R. Taylor, and J. M. Thornton. 1994. A model recognition approach to the prediction of all-helical membrane protein structure and topology. Biochemistry. 33:3038-3049.
    • (1994) Biochemistry , vol.33 , pp. 3038-3049
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 69
    • 0028803306 scopus 로고
    • A. FTIR spectroscopy reveals microscopic structural changes of the protein around the rhodopsin chromophore upon photoisomerization
    • Kandori, H., and A. Maeda. 1995. A. FTIR spectroscopy reveals microscopic structural changes of the protein around the rhodopsin chromophore upon photoisomerization. Biochemistry. 34:14220-14229.
    • (1995) Biochemistry , vol.34 , pp. 14220-14229
    • Kandori, H.1    Maeda, A.2
  • 70
    • 0028287273 scopus 로고
    • Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmeniosa
    • Kaushal, S., and H. G. Khorana. 1994. Structure and function in rhodopsin. 7. Point mutations associated with autosomal dominant retinitis pigmeniosa. Biochemistry. 33:6121-6128.
    • (1994) Biochemistry , vol.33 , pp. 6121-6128
    • Kaushal, S.1    Khorana, H.G.2
  • 72
    • 0017461195 scopus 로고
    • Solvent effects on the spectra of retinal Schiff bases. I. Models for the bathochromic shift of the chromophore spectrum in visual pigments
    • Kliger, D. S., S. J. Milder, and E. A. Dratz. 1977. Solvent effects on the spectra of retinal Schiff bases. I. Models for the bathochromic shift of the chromophore spectrum in visual pigments. Photochem. Photobiol. 25:277-286.
    • (1977) Photochem. Photobiol. , vol.25 , pp. 277-286
    • Kliger, D.S.1    Milder, S.J.2    Dratz, E.A.3
  • 74
    • 0027444691 scopus 로고
    • A single residue, aspartic acid 95, in the delta opioid receptor specifies selective high affinity agonist binding
    • Kong, H., K. Raynor, K. Yasuda, S. T. Moe, P. S. Portoghese, G. I. Bell, and T. Reisine. 1993b. A single residue, aspartic acid 95, in the delta opioid receptor specifies selective high affinity agonist binding. J. Biol. Chem. 268:23055-23058.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23055-23058
    • Kong, H.1    Raynor, K.2    Yasuda, K.3    Moe, S.T.4    Portoghese, P.S.5    Bell, G.I.6    Reisine, T.7
  • 75
    • 0028301829 scopus 로고
    • Fourier transform infrared study of the rod outer segment disk and plasma membranes of venebrate retina
    • Lamba, O. P., D. Borchman, and P. J. O'Brien. 1994. Fourier transform infrared study of the rod outer segment disk and plasma membranes of venebrate retina. Biochemistry. 33:1704-1712.
    • (1994) Biochemistry , vol.33 , pp. 1704-1712
    • Lamba, O.P.1    Borchman, D.2    O'Brien, P.J.3
  • 76
    • 0028944310 scopus 로고
    • Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precocious puberty
    • Laue, L., W. Y. Chan, A. J. Hsueh, M. Kudo, S. Y. Hsu, S. M. Wu, L. Blomberg, and G. B. Cutler, Jr. 1995. Genetic heterogeneity of constitutively activating mutations of the human luteinizing hormone receptor in familial male-limited precocious puberty. Proc. Natl. Acad. Sci. USA. 92:1906-1910.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1906-1910
    • Laue, L.1    Chan, W.Y.2    Hsueh, A.J.3    Kudo, M.4    Hsu, S.Y.5    Wu, S.M.6    Blomberg, L.7    Cutler G.B., Jr.8
  • 77
    • 0001631281 scopus 로고
    • In situ microspectrophotometric studies on the pigment of single retinal rods
    • Liebman, P. A. 1962. In situ microspectrophotometric studies on the pigment of single retinal rods. Biophys. J. 2:161-178.
    • (1962) Biophys. J. , vol.2 , pp. 161-178
    • Liebman, P.A.1
  • 78
    • 0028316890 scopus 로고
    • What makes red visual pigments red? A resonance Raman microprobe study of retinal chromophore structure in iodopsin
    • Lin, S. W., Y. Imamoto, Y. Fukada, Y. Shichida, T. Yoshizawa, and R. A. Mathies. 1994. What makes red visual pigments red? A resonance Raman microprobe study of retinal chromophore structure in iodopsin. Biochemistry. 33:2151-2160.
    • (1994) Biochemistry , vol.33 , pp. 2151-2160
    • Lin, S.W.1    Imamoto, Y.2    Fukada, Y.3    Shichida, Y.4    Yoshizawa, T.5    Mathies, R.A.6
  • 79
    • 0029756165 scopus 로고    scopus 로고
    • Specific trypiopban UV-absorbance changes are probes of the transition of rhodopsin to its active state
    • Lin, S. W., and T. P. Sakmar. 1996. Specific trypiopban UV-absorbance changes are probes of the transition of rhodopsin to its active state. Biochemistry. 35:11149-11159.
    • (1996) Biochemistry , vol.35 , pp. 11149-11159
    • Lin, S.W.1    Sakmar, T.P.2
  • 80
    • 0026750971 scopus 로고
    • Resonance Raman microprobe spectroscopy of rhodopsin mutants: Effect of substitutions in the third transmembrane helix
    • Lin, S. W., T. P. Sakmar, R. R. Franke, H. G. Khorana, and R. A. Mathies. 1992. Resonance Raman microprobe spectroscopy of rhodopsin mutants: effect of substitutions in the third transmembrane helix. Biochemistry. 31:5105-5111.
    • (1992) Biochemistry , vol.31 , pp. 5105-5111
    • Lin, S.W.1    Sakmar, T.P.2    Franke, R.R.3    Khorana, H.G.4    Mathies, R.A.5
  • 81
    • 0039227396 scopus 로고
    • The binding site of opsin based on analogue studies with isomeric, fluorinated, alkylated, and other modified retinals
    • M. I. Dawson and W. H. Okamura, editors. CRC Press, Boca Raton, FL
    • Liu, R. S. H., and A. Asato. 1989. The binding site of opsin based on analogue studies with isomeric, fluorinated, alkylated, and other modified retinals. In Chemistry and Biology of Synthetic Retinoids. M. I. Dawson and W. H. Okamura, editors. CRC Press, Boca Raton, FL. 52-75.
    • (1989) Chemistry and Biology of Synthetic Retinoids , pp. 52-75
    • Liu, R.S.H.1    Asato, A.2
  • 82
    • 0000812503 scopus 로고
    • The nature of restrictions in the binding site of rhodopsin. A model study
    • Liu, R. S. H., A. Asato, M. Denny, and D. Mead. 1984. The nature of restrictions in the binding site of rhodopsin. A model study. J. Am. Chem. Soc. 106:8298-8300.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 8298-8300
    • Liu, R.S.H.1    Asato, A.2    Denny, M.3    Mead, D.4
  • 83
    • 0000254592 scopus 로고
    • The shape of a three dimensional binding site of rhodopsin based on molecular modeling analysis of isomeric and other visual pigment analogues. Bioorganic studies of visual pigments
    • Liu, R. S. H., and T. Mirzadegan. 1988. The shape of a three dimensional binding site of rhodopsin based on molecular modeling analysis of isomeric and other visual pigment analogues. Bioorganic studies of visual pigments. J. Am. Chem. Soc. 110:8617-8623.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 8617-8623
    • Liu, R.S.H.1    Mirzadegan, T.2
  • 84
    • 0029096818 scopus 로고
    • Mutational analysis of the relative orientation of transmembrane helices I and VII in G-protein-coupled receptors
    • Liu, J., T. Schöneberg, M. van Rhee, and J. Wess. 1995. Mutational analysis of the relative orientation of transmembrane helices I and VII in G-protein-coupled receptors. J. Biol. Chem. 270:19532-19539.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19532-19539
    • Liu, J.1    Schöneberg, T.2    Van Rhee, M.3    Wess, J.4
  • 85
    • 0026813599 scopus 로고
    • Refinement of the spatial structure of the gramicidin A transmembrane ion-channel
    • Lomize, A. L., V. Yu. Orekhov, and A. S. Arseniev. 1992. Refinement of the spatial structure of the gramicidin A transmembrane ion-channel. Bioorg. Khim. 18:182-200.
    • (1992) Bioorg. Khim. , vol.18 , pp. 182-200
    • Lomize, A.L.1    Orekhov, V.Yu.2    Arseniev, A.S.3
  • 86
    • 0027365358 scopus 로고
    • Water structural changes in lumirhodopsin, metarhodopsin I and metarhodopsin II upon photolysis of bovine rhodopsin: Analysis by Fourier transform infrared spectroscopy
    • Maeda, A., Y. J. Ohkita, J. Sasaki, Y. Shichida, and T. Yoshizawa. 1993. Water structural changes in lumirhodopsin, metarhodopsin I and metarhodopsin II upon photolysis of bovine rhodopsin: analysis by Fourier transform infrared spectroscopy. Biochemistry. 32:12033-12038.
    • (1993) Biochemistry , vol.32 , pp. 12033-12038
    • Maeda, A.1    Ohkita, Y.J.2    Sasaki, J.3    Shichida, Y.4    Yoshizawa, T.5
  • 87
    • 0018794337 scopus 로고
    • Formation of 7-cis and 13-cis retinal pigments by irradiating squid rhodopsin
    • Maeda, A., Y. Shichida, and T. Yoshizawa. 1979. Formation of 7-cis and 13-cis retinal pigments by irradiating squid rhodopsin. Biochemistry. 18:1449-1453.
    • (1979) Biochemistry , vol.18 , pp. 1449-1453
    • Maeda, A.1    Shichida, Y.2    Yoshizawa, T.3
  • 88
    • 0020762066 scopus 로고
    • I. Study of the molecular organization of visual rhodopsin in photoreceptor membranes by limited proteolysis
    • Martynov, V. I., M. B. Kostina, M. Y. Feigina, and A. Miroshnikov. 1983. I. Study of the molecular organization of visual rhodopsin in photoreceptor membranes by limited proteolysis. Bioorg. Khim. 9:735-745.
    • (1983) Bioorg. Khim. , vol.9 , pp. 735-745
    • Martynov, V.I.1    Kostina, M.B.2    Feigina, M.Y.3    Miroshnikov, A.4
  • 90
    • 0001718556 scopus 로고
    • Retinal has highly dipolar vertically excited singlet state: Implication for vision
    • Mathies, R., and L. Stryer. 1976. Retinal has highly dipolar vertically excited singlet state: implication for vision. Proc. Natl. Acad. Sci. USA. 73:2169-2173.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2169-2173
    • Mathies, R.1    Stryer, L.2
  • 91
    • 0026319603 scopus 로고
    • Stabilization of functional proteins by introduction of multiple disulfide bonds
    • Matsumura, M., and B. W. Matthews. 1991. Stabilization of functional proteins by introduction of multiple disulfide bonds. Methods Enzymol. 202:336-356.
    • (1991) Methods Enzymol. , vol.202 , pp. 336-356
    • Matsumura, M.1    Matthews, B.W.2
  • 92
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K., and J. M. Thornton. 1994. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 93
    • 0030028517 scopus 로고    scopus 로고
    • Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin
    • Mizobe, T., M. Maze, V. Lam, S. Suryanarayana, and B. K. Kobilka. 1996. Arrangement of transmembrane domains in adrenergic receptors. Similarity to bacteriorhodopsin. J. Biol. Chem. 271:2387-2389.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2387-2389
    • Mizobe, T.1    Maze, M.2    Lam, V.3    Suryanarayana, S.4    Kobilka, B.K.5
  • 95
    • 5944250450 scopus 로고
    • Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids
    • Momany, F. A., R. F. McGuire, A. W. Burgess, and H. A. Scheraga. 1975. Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids. J. Phys. Chem. 79:2361-2181.
    • (1975) J. Phys. Chem. , vol.79 , pp. 2361-12181
    • Momany, F.A.1    McGuire, R.F.2    Burgess, A.W.3    Scheraga, H.A.4
  • 96
    • 84986505827 scopus 로고
    • Validation of the general purpose QUANTA3.2/CHARMm force field
    • Momany, F. A., and R. Rone. 1992. Validation of the general purpose QUANTA3.2/CHARMm force field. J. Comput. Chem. 13:888-900.
    • (1992) J. Comput. Chem. , vol.13 , pp. 888-900
    • Momany, F.A.1    Rone, R.2
  • 97
    • 0030028756 scopus 로고    scopus 로고
    • Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants
    • Monnot, C., C. Bihoreau, S. Conchon, K. M. Curnow, P. Corvol, and E. Clauser. 1996. Polar residues in the transmembrane domains of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants. J. Biol. Chem. 271:1507-1513.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1507-1513
    • Monnot, C.1    Bihoreau, C.2    Conchon, S.3    Curnow, K.M.4    Corvol, P.5    Clauser, E.6
  • 98
    • 0028955505 scopus 로고
    • Predicting the helix packing of globular proteins by self-correcting distance geometry
    • Mumenthaler, C., and W. Braun. 1995. Predicting the helix packing of globular proteins by self-correcting distance geometry. Protein Sci. 4:863-871.
    • (1995) Protein Sci. , vol.4 , pp. 863-871
    • Mumenthaler, C.1    Braun, W.2
  • 99
    • 0027479161 scopus 로고
    • OB(oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A. G. 1993. OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EMBO J. 12:861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 100
    • 0029950031 scopus 로고    scopus 로고
    • Structural classification of proteins: New superfamilies
    • Murzin, A. G. 1996. Structural classification of proteins: new superfamilies. Curr. Opin. Struct. Biol. 6:386-394.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 386-394
    • Murzin, A.G.1
  • 101
    • 0025050478 scopus 로고
    • Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal
    • Nakayama, T. A., and H. G. Khorana. 1990. Orientation of retinal in bovine rhodopsin determined by cross-linking using a photoactivatable analog of 11-cis-retinal. J. Biol. Chem. 265:15762-15769.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15762-15769
    • Nakayama, T.A.1    Khorana, H.G.2
  • 102
    • 0025761854 scopus 로고
    • Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin
    • Nakayama, T. A., and H. G. Khorana. 1991. Mapping of the amino acids in membrane-embedded helices that interact with the retinal chromophore in bovine rhodopsin. J. Biol. Chem. 266:4269-4275.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4269-4275
    • Nakayama, T.A.1    Khorana, H.G.2
  • 103
    • 0025012994 scopus 로고
    • Determinants of visual pigment absorbance: Role of charged amino acid in the putative transmembrane segments
    • Nathans, J. 1990a. Determinants of visual pigment absorbance: role of charged amino acid in the putative transmembrane segments. Biochemistry: 29:937-942.
    • (1990) Biochemistry , vol.29 , pp. 937-942
    • Nathans, J.1
  • 104
    • 0025162902 scopus 로고
    • Determinants of visual pigment absorbance: Identification of the retinylidene Schiff's base counterion in bovine rhodopsin
    • Nathans, J. 1990b. Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin. Biochemistry. 29:9746-9752.
    • (1990) Biochemistry , vol.29 , pp. 9746-9752
    • Nathans, J.1
  • 105
    • 0001228323 scopus 로고
    • A common motif in G-protein-coupled seven transmembrane helix receptors
    • Oliveira, L., A. C. M. Paiva, and G. Vriend. 1993. A common motif in G-protein-coupled seven transmembrane helix receptors. J. Comput. Aided Mol. Des. 7:649-658.
    • (1993) J. Comput. Aided Mol. Des. , vol.7 , pp. 649-658
    • Oliveira, L.1    Paiva, A.C.M.2    Vriend, G.3
  • 106
    • 0026772266 scopus 로고
    • The ligand-binding domain of rhodopsin and other G-protein-linked receptors
    • Oprian, D. D. 1992. The ligand-binding domain of rhodopsin and other G-protein-linked receptors. J. Bioenerg. Biomembr. 24:211-217.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 211-217
    • Oprian, D.D.1
  • 107
    • 0016289846 scopus 로고
    • Resonance Raman spectroscopy of rhodopsin in retinal disk membranes
    • Oseroff, A. R., and R. H. Callender. 1974. Resonance Raman spectroscopy of rhodopsin in retinal disk membranes. Biochemistry. 13:4243-4248.
    • (1974) Biochemistry , vol.13 , pp. 4243-4248
    • Oseroff, A.R.1    Callender, R.H.2
  • 108
    • 0023215761 scopus 로고
    • Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: Implication for chromophore structure and environment
    • Palings, I., J. A. Pardoen, E. van der Berg, C. Winkel, J. Lugtenburg, and R. A. Mathies. 1987. Assignment of fingerprint vibrations in the resonance Raman spectra of rhodopsin, isorhodopsin, and bathorhodopsin: implication for chromophore structure and environment. Biochemistry. 26:2544-2656.
    • (1987) Biochemistry , vol.26 , pp. 2544-2656
    • Palings, I.1    Pardoen, J.A.2    Van Der Berg, E.3    Winkel, C.4    Lugtenburg, J.5    Mathies, R.A.6
  • 109
    • 0028279520 scopus 로고
    • Prediction of transmembrane segments in proteins utilising multiple sequence alignments
    • Persson, B., and P. Argos. 1994. Prediction of transmembrane segments in proteins utilising multiple sequence alignments. J. Mol. Biol. 237: 182-192.
    • (1994) J. Mol. Biol. , vol.237 , pp. 182-192
    • Persson, B.1    Argos, P.2
  • 110
    • 0028012105 scopus 로고
    • Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors
    • Pittel, Z., and J. Wess. 1994. Intramolecular interactions in muscarinic acetylcholine receptors studied with chimeric m2/m5 receptors. Mol. Pharmacol. 45:61-64.
    • (1994) Mol. Pharmacol. , vol.45 , pp. 61-64
    • Pittel, Z.1    Wess, J.2
  • 112
    • 0027170277 scopus 로고
    • The regulation of the binding affinity of the luteinizing hormone/choriogonadotropin receptor by sodium ions is mediated by a highly conserved aspartate located in the second transmembrane domain of G-protein-coupled receptors
    • Quintana, J., H. Wang, and M. Ascoli. 1993. The regulation of the binding affinity of the luteinizing hormone/choriogonadotropin receptor by sodium ions is mediated by a highly conserved aspartate located in the second transmembrane domain of G-protein-coupled receptors. Mol. Endocrinol. 7:767-775.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 767-775
    • Quintana, J.1    Wang, H.2    Ascoli, M.3
  • 113
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao, V. R., G. B. Cohen, and D. D. Oprian. 1994. Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature. 367:639-642.
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 114
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G-protein-coupled receptors
    • Rao, V. R., and D. D. Oprian. 1996. Activating mutations of rhodopsin and other G-protein-coupled receptors. Annu. Rev. Biophys. Biomol. Struct. 25:287-314.
    • (1996) Annu. Rev. Biophys. Biomol. Struct. , vol.25 , pp. 287-314
    • Rao, V.R.1    Oprian, D.D.2
  • 115
    • 0027364707 scopus 로고
    • Fourier transform infrared difference spectroscopy of rhodopsin mutants: Light activation of rhodopsin causes hydrogen-bonding changes in residue aspartic acid-83 during Meta II formation
    • Rath, P., L. L. J. DeCaluwé. P. H. M. Bovee-Geurts, W. J. DeGrip, and K. J. Rothschild. 1993. Fourier transform infrared difference spectroscopy of rhodopsin mutants: light activation of rhodopsin causes hydrogen-bonding changes in residue aspartic acid-83 during Meta II formation. Biochemistry. 32:10277-10282.
    • (1993) Biochemistry , vol.32 , pp. 10277-10282
    • Rath, P.1    DeCaluwé, L.L.J.2    Bovee-Geurts, P.H.M.3    DeGrip, W.J.4    Rothschild, K.J.5
  • 116
    • 0027443076 scopus 로고
    • Formation of the Meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin
    • Resek, J. F., Z. T. Farahbakhsh, W. L. Hubbell, and H. G. Khorana. 1993. Formation of the Meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin. Biochemistry. 32:12025-12032.
    • (1993) Biochemistry , vol.32 , pp. 12025-12032
    • Resek, J.F.1    Farahbakhsh, Z.T.2    Hubbell, W.L.3    Khorana, H.G.4
  • 117
    • 0029012391 scopus 로고
    • Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements
    • Ridge, K. D., C. Zhang, and H. G. Khorana. 1995. Mapping of the amino acids in the cytoplasmic loop connecting helices C and D in rhodopsin. Chemical reactivity in the dark state following single cysteine replacements. Biochemistry. 34:8804-8811.
    • (1995) Biochemistry , vol.34 , pp. 8804-8811
    • Ridge, K.D.1    Zhang, C.2    Khorana, H.G.3
  • 118
    • 0028902788 scopus 로고
    • Transmembrane helices predicted at 95% accuracy
    • Rost, B., R. Casadio, P. Fariselli, and C. Sander. 1995. Transmembrane helices predicted at 95% accuracy. Protein Sci. 4:521-533.
    • (1995) Protein Sci. , vol.4 , pp. 521-533
    • Rost, B.1    Casadio, R.2    Fariselli, P.3    Sander, C.4
  • 119
    • 85005586843 scopus 로고
    • Properties and photoactivity of rhodopsin mutants
    • Sakmar, T. P., and K. Fahmy. 1995. Properties and photoactivity of rhodopsin mutants. Isr. J. Chem. 35:325-337.
    • (1995) Isr. J. Chem. , vol.35 , pp. 325-337
    • Sakmar, T.P.1    Fahmy, K.2
  • 120
    • 0343177634 scopus 로고
    • Glutamic acid-113 serves as a retinylidene Schiff base counterion in bovine rhodopsin
    • Sakmar, T. P., R. R. Franke, and H. G. Khorana. 1989. Glutamic acid-113 serves as a retinylidene Schiff base counterion in bovine rhodopsin. Proc. Natl. Acad. Sci. USA. 86:8309-8313.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8309-8313
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 121
    • 0026341233 scopus 로고
    • The role of the retinylidene Schiff base counterion in rhodopsin in determining wave-length absorbance and Schiff base pKa
    • Sakmar, T. P., R. R. Franke, and H. G. Khorana. 1991. The role of the retinylidene Schiff base counterion in rhodopsin in determining wave-length absorbance and Schiff base pKa. Proc. Natl. Acad. Sci. USA. 88:3079-3083.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3079-3083
    • Sakmar, T.P.1    Franke, R.R.2    Khorana, H.G.3
  • 124
    • 0029556994 scopus 로고
    • Projection structure of frog rhodopsin in two crystal forms
    • Schertler, G. F. X., and P. A. Hargrave. 1995. Projection structure of frog rhodopsin in two crystal forms. Proc. Natl. Acad. Sci. USA. 92: 11578-11582.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11578-11582
    • Schertler, G.F.X.1    Hargrave, P.A.2
  • 126
    • 4243676201 scopus 로고
    • The structure of rhodopsin obtained by cryo-electron microscopy to 7 Å resolution
    • Schertler, G. F. X., V. M. Unger, and P. A. Hargrave. 1995. The structure of rhodopsin obtained by cryo-electron microscopy to 7 Å resolution. Biophys. J. 68:A21.
    • (1995) Biophys. J. , vol.68
    • Schertler, G.F.X.1    Unger, V.M.2    Hargrave, P.A.3
  • 127
    • 0027190359 scopus 로고
    • Projection structure of rhodopsin
    • Schertler, G. F. X., C. Villa, and R. Henderson. 1993. Projection structure of rhodopsin. Nature. 362:770-772.
    • (1993) Nature , vol.362 , pp. 770-772
    • Schertler, G.F.X.1    Villa, C.2    Henderson, R.3
  • 128
    • 0001761402 scopus 로고
    • Structure-function relationships in the membrane channel porin as based on 1.8. Å resolution crystal structure
    • A. Pullman, J. Jortner, B. Pullman, editors. Kluwer Academic Publishers, Netherlands
    • Schultz, G. E. 1992. Structure-function relationships in the membrane channel porin as based on 1.8. Å resolution crystal structure. In Membrane Proteins: Structures, Interactions and Models. A. Pullman, J. Jortner, B. Pullman, editors. Kluwer Academic Publishers, Netherlands. 403-412.
    • (1992) Membrane Proteins: Structures, Interactions and Models , pp. 403-412
    • Schultz, G.E.1
  • 129
    • 0027026391 scopus 로고
    • Magic angle spinning NMR studies on the metarhodopsin II intermediate of bovine rhodopsin: Evidence for an unprotonated Schiff base
    • Smith, S. O., H. De Groot, R. Gebhard, and J. Lugtenburg. 1992. Magic angle spinning NMR studies on the metarhodopsin II intermediate of bovine rhodopsin: evidence for an unprotonated Schiff base. Photochem. Photobiol. 56:1035-1039.
    • (1992) Photochem. Photobiol. , vol.56 , pp. 1035-1039
    • Smith, S.O.1    De Groot, H.2    Gebhard, R.3    Lugtenburg, J.4
  • 132
    • 0028262380 scopus 로고
    • Two hypotheses - One answer. Sequence comparison does not support an evolutionary link between halobacterial retinal proteins including bacteriorhodopsin and eukaryotic G-protein-coupled receptors
    • Soppa, J. 1994. Two hypotheses - one answer. Sequence comparison does not support an evolutionary link between halobacterial retinal proteins including bacteriorhodopsin and eukaryotic G-protein-coupled receptors. FEBS Lett. 342:7-11.
    • (1994) FEBS Lett. , vol.342 , pp. 7-11
    • Soppa, J.1
  • 133
    • 0027335795 scopus 로고
    • pKa of the protonated Schiff base of bovine rhodopsin. A study with artificial pigments
    • Steinberg, G., M. Ottolenghi, and M. Sheves. 1993. pKa of the protonated Schiff base of bovine rhodopsin. A study with artificial pigments. Biophys. J. 64:1499-1502.
    • (1993) Biophys. J. , vol.64 , pp. 1499-1502
    • Steinberg, G.1    Ottolenghi, M.2    Sheves, M.3
  • 134
    • 0026592867 scopus 로고
    • Identification of intramolecular interactions in adrenergic receptors
    • Suryanarayana, S., M. von Zastrow, and B. K. Kobilka. 1992. Identification of intramolecular interactions in adrenergic receptors. J. Biol. Chem. 267:21991-21994.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21991-21994
    • Suryanarayana, S.1    Von Zastrow, M.2    Kobilka, B.K.3
  • 135
    • 0028175436 scopus 로고
    • A method for α-helical integral membrane protein fold prediction
    • Taylor, W. R., D. T. Jones, and N. M. Green. 1994. A method for α-helical integral membrane protein fold prediction. Proteins Struct. Funct. Genet. 18:281-294.
    • (1994) Proteins Struct. Funct. Genet. , vol.18 , pp. 281-294
    • Taylor, W.R.1    Jones, D.T.2    Green, N.M.3
  • 136
    • 0029873472 scopus 로고    scopus 로고
    • Construction of a high affinity zinc switch in the κ-opioid receptor
    • Thirstrup, K., C. E. Elling, S. A. Hjorth, and T. W. Schwartz. 1996. Construction of a high affinity zinc switch in the κ-opioid receptor. J. Biol. Chem. 271:7875-7878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7875-7878
    • Thirstrup, K.1    Elling, C.E.2    Hjorth, S.A.3    Schwartz, T.W.4
  • 137
    • 0020079867 scopus 로고
    • Transverse location of the retinal chromophore of rhodopsin in rod outer segment disc membranes
    • Thomas, D. D., and L. Stryer. 1982. Transverse location of the retinal chromophore of rhodopsin in rod outer segment disc membranes. J. Mol. Biol. 154:145-157.
    • (1982) J. Mol. Biol. , vol.154 , pp. 145-157
    • Thomas, D.D.1    Stryer, L.2
  • 138
    • 25344473118 scopus 로고
    • Localization of the transmembrane helices in the three-dimentional structure of frog rhodopsin
    • Unger, V. M., P. A. Hargrave, and G. F. X. Schertler. 1995. Localization of the transmembrane helices in the three-dimentional structure of frog rhodopsin. Biophys. J. 68:A330.
    • (1995) Biophys. J. , vol.68
    • Unger, V.M.1    Hargrave, P.A.2    Schertler, G.F.X.3
  • 139
    • 0028962270 scopus 로고
    • Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy
    • Unger, V. M., and G. F. X. Schertler. 1995. Low resolution structure of bovine rhodopsin determined by electron cryo-microscopy. Biophys. J. 68:1776-1786.
    • (1995) Biophys. J. , vol.68 , pp. 1776-1786
    • Unger, V.M.1    Schertler, G.F.X.2
  • 140
    • 0001698852 scopus 로고
    • Chromophores of insect visual pigments
    • Vogt, K. 1987. Chromophores of insect visual pigments. Photobiochem. Photobiophys. 2(Suppl.):273-296.
    • (1987) Photobiochem. Photobiophys. , vol.2 , Issue.SUPPL. , pp. 273-296
    • Vogt, K.1
  • 141
    • 0029867179 scopus 로고    scopus 로고
    • Principles of helix-helix packing in proteins: The helical lattice superposition model
    • Walther, D., F. Eisenhaber, and P. Argos. 1996. Principles of helix-helix packing in proteins: the helical lattice superposition model. J. Mol. Biol. 255:536-553.
    • (1996) J. Mol. Biol. , vol.255 , pp. 536-553
    • Walther, D.1    Eisenhaber, F.2    Argos, P.3
  • 143
    • 0027723278 scopus 로고
    • Rhodopsin activation: Effect on the Metarhodopsin I-Metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments
    • Weitz, C. J., and J. Nathans. 1993. Rhodopsin activation: effect on the Metarhodopsin I-Metarhodopsin II equilibrium of neutralization or introduction of charged amino acids within putative transmembrane segments. Biochemistry. 32:14176-14182.
    • (1993) Biochemistry , vol.32 , pp. 14176-14182
    • Weitz, C.J.1    Nathans, J.2
  • 145
    • 0028812838 scopus 로고
    • Structure of the third cytoplasmic loop of bovine rhodopsin
    • Yeagle, P. L., J. L. Alderfer, and A. D. Albert. 1995a. Structure of the third cytoplasmic loop of bovine rhodopsin. Biochemistry. 34:14621-14625.
    • (1995) Biochemistry , vol.34 , pp. 14621-14625
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 146
    • 0029391341 scopus 로고
    • Structure of the carboxy-terminal domain of bovine rhodopsin
    • Yeagle, P. L., J. L. Alderfer, and A. D. Albert. 1995b. Structure of the carboxy-terminal domain of bovine rhodopsin. Nature Struct. Biol. 2:832-834.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 832-834
    • Yeagle, P.L.1    Alderfer, J.L.2    Albert, A.D.3
  • 147
    • 0028822684 scopus 로고
    • General method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins
    • Yu, H., M. Kono, T. D. McKee, and D. D. Oprian. 1995. General method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins. Biochemistry. 34:14963-14969.
    • (1995) Biochemistry , vol.34 , pp. 14963-14969
    • Yu, H.1    Kono, M.2    McKee, T.D.3    Oprian, D.D.4
  • 150
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side-chain on the absorption maximum of visual pigments
    • Zhukovsky, E. A., and D. D. Oprian. 1989. Effect of carboxylic acid side-chain on the absorption maximum of visual pigments. Science. 246:928-930.
    • (1989) Science , vol.246 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2
  • 151
    • 0026475571 scopus 로고
    • Changing the location of the Schiff base counterion in rhodopsin
    • Zhukovsky, E. A., P. R. Robinson, and D. D. Oprian. 1992. Changing the location of the Schiff base counterion in rhodopsin. Biochemistry. 31: 10400-10405.
    • (1992) Biochemistry , vol.31 , pp. 10400-10405
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 152
    • 0027462158 scopus 로고
    • Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition
    • Zvyaga, T., K. C. Min, M. Beck, and T. P. Sakmar. 1993. Movement of the retinylidene Schiff base counterion in rhodopsin by one helix turn reverses the pH dependence of the metarhodopsin I to metarhodopsin II transition. J. Biol. Chem. 268:4661-4667.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4661-4667
    • Zvyaga, T.1    Min, K.C.2    Beck, M.3    Sakmar, T.P.4


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