메뉴 건너뛰기




Volumn 44, Issue 7, 2005, Pages 2419-2431

Agonist-induced conformational changes in thyrotropin-releasing hormone receptor type I: Disulfide cross-linking and molecular modeling approaches

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; CHEMICAL BONDS; COMPUTER SIMULATION; CONFORMATIONS; CROSSLINKING; HYDRATION; MATHEMATICAL MODELS; MOLECULAR DYNAMICS; MUTAGENESIS; SUBSTITUTION REACTIONS;

EID: 14044251558     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048808+     Document Type: Article
Times cited : (23)

References (68)
  • 2
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens, D. L., Altenbach, C., Yang, K., Hubbell, W. L., and Khorana, H. G. (1996) Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin, Science 274, 768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 3
    • 0029680797 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels
    • Yang, K., Farrens, D. L., Altenbach, C., Farahbakhsh, Z. T., Hubbell, W. L., and Khorana, H. G. (1996) Structure and function in rhodopsin. Cysteines 65 and 316 are in proximity in a rhodopsin mutant as indicated by disulfide formation and interactions between attached spin labels, Biochemistry 35, 14040-14046.
    • (1996) Biochemistry , vol.35 , pp. 14040-14046
    • Yang, K.1    Farrens, D.L.2    Altenbach, C.3    Farahbakhsh, Z.T.4    Hubbell, W.L.5    Khorana, H.G.6
  • 4
    • 0031446595 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state
    • Kim, J. M., Altenbach, C., Thurmond, R. L., Khorana, H. G., and Hubbell, W. L. (1997) Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state, Proc. Natl. Acad. Sci. U.S.A. 94, 14273-14278.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14273-14278
    • Kim, J.M.1    Altenbach, C.2    Thurmond, R.L.3    Khorana, H.G.4    Hubbell, W.L.5
  • 5
    • 0033580636 scopus 로고    scopus 로고
    • Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin
    • Struthers, M., Yu, H., Kono, M., and Oprian, D. D. (1999) Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin, Biochemistry 38, 6597-6603.
    • (1999) Biochemistry , vol.38 , pp. 6597-6603
    • Struthers, M.1    Yu, H.2    Kono, M.3    Oprian, D.D.4
  • 6
    • 0033554440 scopus 로고    scopus 로고
    • Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin
    • Yu, H., and Oprian, D. D. (1999) Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin, Biochemistry 38, 12033-12040.
    • (1999) Biochemistry , vol.38 , pp. 12033-12040
    • Yu, H.1    Oprian, D.D.2
  • 7
    • 0033522912 scopus 로고    scopus 로고
    • Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation
    • Zeng, F. Y., Hopp, A., Soldner, A., and Wess, J. (1999) Use of a disulfide cross-linking strategy to study muscarinic receptor structure and mechanisms of activation, J. Biol. Chem. 274, 16629-16640.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16629-16640
    • Zeng, F.Y.1    Hopp, A.2    Soldner, A.3    Wess, J.4
  • 8
    • 0037127315 scopus 로고    scopus 로고
    • Conformational changes that occur during M3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy
    • Ward, S. D., Hamdan, F. F., Bloodworth, L. M., and Wess, J. (2002) Conformational changes that occur during M3 muscarinic acetylcholine receptor activation probed by the use of an in situ disulfide cross-linking strategy, J. Biol. Chem. 277, 2247-2257.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2247-2257
    • Ward, S.D.1    Hamdan, F.F.2    Bloodworth, L.M.3    Wess, J.4
  • 9
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • Sheikh, S. P., Zvyaga, T. A., Lichtarge, O., Sakmar, T. P., and Bourne, H. R. (1996) Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F, Nature 383, 347-350.
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1    Zvyaga, T.A.2    Lichtarge, O.3    Sakmar, T.P.4    Bourne, H.R.5
  • 10
    • 0033546197 scopus 로고    scopus 로고
    • Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor, Zn(II) bridges between helices III and VI block activation
    • Sheikh, S. P., Vilardarga, J. P., Baranski, T. J., Lichtarge, O., Iiri, T., Meng, E. C., Nissenson, R. A., and Bourne, H. R. (1999) Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation, J. Biol. Chem. 274, 17033-17041.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17033-17041
    • Sheikh, S.P.1    Vilardarga, J.P.2    Baranski, T.J.3    Lichtarge, O.4    Iiri, T.5    Meng, E.C.6    Nissenson, R.A.7    Bourne, H.R.8
  • 11
    • 0034095059 scopus 로고    scopus 로고
    • A network of conserved intramolecular contacts defines the off-state of the transmembrane switch mechanism in a seven-transmembrane receptor
    • Lu, Z. L., and Hulme, E. C. (2000) A network of conserved intramolecular contacts defines the off-state of the transmembrane switch mechanism in a seven-transmembrane receptor, J. Biol. Chem. 275, 5682-5686.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5682-5686
    • Lu, Z.L.1    Hulme, E.C.2
  • 12
    • 0030611331 scopus 로고    scopus 로고
    • Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment
    • Javitch, J. A., Fu, D., Liapakis, G., and Chen, J. (1997) Constitutive activation of the beta2 adrenergic receptor alters the orientation of its sixth membrane-spanning segment, J. Biol. Chem. 272, 18546-18549.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18546-18549
    • Javitch, J.A.1    Fu, D.2    Liapakis, G.3    Chen, J.4
  • 13
    • 0028856707 scopus 로고
    • Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes
    • Gether, U., Lin, S., and Kobilka, B. K. (1995) Fluorescent labeling of purified beta 2 adrenergic receptor. Evidence for ligand-specific conformational changes, J. Biol. Chem. 270, 28268-28275.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28268-28275
    • Gether, U.1    Lin, S.2    Kobilka, B.K.3
  • 14
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • Gether, U., Ballesteros, J. A., Seifert, R., Sanders-Bush, E., Weinstein, H., and Kobilka, B. K. (1997) Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility, J. Biol. Chem. 272, 2587-2590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 15
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor
    • Gether, U., Lin, S., Ghanouni, P., Ballesteros, J. A., Weinstein, H., and Kobilka, B. K. (1997) Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor, EMBO J. 16, 6737-6747.
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1    Lin, S.2    Ghanouni, P.3    Ballesteros, J.A.4    Weinstein, H.5    Kobilka, B.K.6
  • 17
    • 0028158607 scopus 로고
    • Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidylinositol hydrolysis
    • Bluml, K., Mutschler, E., and Wess, J. (1994) Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidylinositol hydrolysis, J. Biol. Chem. 269, 402-405.
    • (1994) J. Biol. Chem. , vol.269 , pp. 402-405
    • Bluml, K.1    Mutschler, E.2    Wess, J.3
  • 18
    • 0028244065 scopus 로고
    • Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C
    • Bluml, K., Mutschler, E., and Wess, J. (1994) Functional role of a cytoplasmic aromatic amino acid in muscarinic receptor-mediated activation of phospholipase C, J. Biol. Chem. 269, 11537-11541.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11537-11541
    • Bluml, K.1    Mutschler, E.2    Wess, J.3
  • 19
    • 0028814543 scopus 로고
    • Structure-function of muscarinic receptor coupling to G Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins
    • Burstein, E. S., Spalding, T. A., Hill-Eubanks, D., and Brann, M. R. (1995) Structure-function of muscarinic receptor coupling to G proteins. Random saturation mutagenesis identifies a critical determinant of receptor affinity for G proteins, J. Biol. Chem. 270, 3141-3146.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3141-3146
    • Burstein, E.S.1    Spalding, T.A.2    Hill-Eubanks, D.3    Brann, M.R.4
  • 20
    • 0030039837 scopus 로고    scopus 로고
    • Structure of a G-protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis
    • Hill-Eubanks, D., Burstein, E. S., Spalding, T. A., Brauner-Osborne, H., and Brann, M. R. (1996) Structure of a G-protein-coupling domain of a muscarinic receptor predicted by random saturation mutagenesis, J. Biol. Chem. 271, 3058-3065.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3058-3065
    • Hill-Eubanks, D.1    Burstein, E.S.2    Spalding, T.A.3    Brauner-Osborne, H.4    Brann, M.R.5
  • 21
    • 0030041761 scopus 로고    scopus 로고
    • Amino acid side chains that define muscarinic receptor/G-protein coupling. Studies of the third intracellular loop
    • Burstein, E. S., Spalding, T. A., and Brann, M. R. (1996) Amino acid side chains that define muscarinic receptor/G-protein coupling. Studies of the third intracellular loop, J. Biol. Chem. 271, 2882-2885.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2882-2885
    • Burstein, E.S.1    Spalding, T.A.2    Brann, M.R.3
  • 22
    • 0033735198 scopus 로고    scopus 로고
    • Juxtamembrane regions in the third intracellular loop of the thyrotropin-releasing hormone receptor type 1 are important for coupling to Gq
    • Buck, F., Wang, W., Harder, S., Brathwaite, C., Bruhn, T. O., and Gershengorn, M. C. (2000) Juxtamembrane regions in the third intracellular loop of the thyrotropin-releasing hormone receptor type 1 are important for coupling to Gq, Endocrinology 141, 3717-3722.
    • (2000) Endocrinology , vol.141 , pp. 3717-3722
    • Buck, F.1    Wang, W.2    Harder, S.3    Brathwaite, C.4    Bruhn, T.O.5    Gershengorn, M.C.6
  • 23
    • 0029589916 scopus 로고
    • Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation
    • Liu, J., Conklin, B. R., Blin, N., Yun, J., and Wess, J. (1995) Identification of a receptor/G-protein contact site critical for signaling specificity and G-protein activation, Proc. Natl. Acad. Sci. U.S.A. 92, 11642-11646.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 11642-11646
    • Liu, J.1    Conklin, B.R.2    Blin, N.3    Yun, J.4    Wess, J.5
  • 24
    • 0029995284 scopus 로고    scopus 로고
    • Molecular mechanisms involved in muscarinic acetylcholine receptor-mediated G protein activation studied by insertion mutagenesis
    • Liu, J., Blin, N., Conklin, B. R., and Wess, J. (1996) Molecular mechanisms involved in muscarinic acetylcholine receptor-mediated G protein activation studied by insertion mutagenesis, J. Biol. Chem. 271, 6172-6178.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6172-6178
    • Liu, J.1    Blin, N.2    Conklin, B.R.3    Wess, J.4
  • 25
    • 0028172426 scopus 로고
    • Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha
    • Taylor, J. M., Jacob-Mosier, G. G., Lawton, R. G., Remmers, A. E., and Neubig, R. R. (1994) Binding of an alpha 2 adrenergic receptor third intracellular loop peptide to G beta and the amino terminus of G alpha, J. Biol. Chem. 269, 27618-27624.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27618-27624
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    Remmers, A.E.4    Neubig, R.R.5
  • 26
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gbeta. A receptor-derived peptide binds to the carboxyl terminus
    • Taylor, J. M., Jacob-Mosier, G. G., Lawton, R. G., VanDort, M., and Neubig, R. R. (1996) Receptor and membrane interaction sites on Gbeta. A receptor-derived peptide binds to the carboxyl terminus, J. Biol. Chem. 271, 3336-3339.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    VanDort, M.4    Neubig, R.R.5
  • 27
    • 0026786080 scopus 로고
    • Rhodopsin/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy
    • Phillips, W. J., and Cerione, R. A. (1992) Rhodopsin/transducin interactions. I. Characterization of the binding of the transducin-beta gamma subunit complex to rhodopsin using fluorescence spectroscopy, J. Biol. Chem. 267, 17032-17039.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17032-17039
    • Phillips, W.J.1    Cerione, R.A.2
  • 28
    • 0028296886 scopus 로고
    • A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation
    • Phillips, W. J., and Cerione, R. A. (1994) A C-terminal peptide of bovine rhodopsin binds to the transducin alpha-subunit and facilitates its activation, Biochem. J. 299 (Pt 2), 351-357.
    • (1994) Biochem. J. , vol.299 , Issue.PART 2 , pp. 351-357
    • Phillips, W.J.1    Cerione, R.A.2
  • 29
    • 0027448975 scopus 로고
    • Decreased levels of internalized thyrotropin-releasing hormone receptors after uncoupling from guanine nucleotide-binding protein and phospholipase-C
    • Nussenzveig, D. R., Heinflink, M., and Gershengorn, M. C. (1993) Decreased levels of internalized thyrotropin-releasing hormone receptors after uncoupling from guanine nucleotide-binding protein and phospholipase-C, Mol. Endocrinol. 7, 1105-1111.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 1105-1111
    • Nussenzveig, D.R.1    Heinflink, M.2    Gershengorn, M.C.3
  • 30
    • 0032407855 scopus 로고    scopus 로고
    • A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation
    • Colson, A. O., Perlman, J. H., Jinsi-Parimoo, A., Nussenzveig, D. R., Osman, R., and Gershengorn, M. C. (1998) A hydrophobic cluster between transmembrane helices 5 and 6 constrains the thyrotropin-releasing hormone receptor in an inactive conformation, Mol. Pharmacol. 54, 968-978.
    • (1998) Mol. Pharmacol. , vol.54 , pp. 968-978
    • Colson, A.O.1    Perlman, J.H.2    Jinsi-Parimoo, A.3    Nussenzveig, D.R.4    Osman, R.5    Gershengorn, M.C.6
  • 31
    • 0035117505 scopus 로고    scopus 로고
    • Minireview: Insights into G protein-coupled receptor function using molecular models
    • Gershengorn, M. C., and Osman, R. (2001) Minireview: Insights into G protein-coupled receptor function using molecular models, Endocrinology 142, 2-10.
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.C.1    Osman, R.2
  • 32
    • 0023224051 scopus 로고
    • Global flexibility in a sensory receptor: A site-directed cross-linking approach
    • Falke, J. J., and Koshland, D. E., Jr. (1987) Global flexibility in a sensory receptor: a site-directed cross-linking approach, Science 237, 1596-1600.
    • (1987) Science , vol.237 , pp. 1596-1600
    • Falke, J.J.1    Koshland Jr., D.E.2
  • 33
    • 0028090254 scopus 로고
    • Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg
    • Lee, G. F., Burrows, G. G., Lebert, M. R., Dutton, D. P., and Hazelbauer, G. L. (1994) Deducing the organization of a transmembrane domain by disulfide cross-linking. The bacterial chemoreceptor Trg, J. Biol. Chem. 269, 29920-29927.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29920-29927
    • Lee, G.F.1    Burrows, G.G.2    Lebert, M.R.3    Dutton, D.P.4    Hazelbauer, G.L.5
  • 34
    • 0029988250 scopus 로고    scopus 로고
    • A general method for determining helix packing in membrane proteins in situ: Helices I and II are close to helix VII in the lactose permease of Escherichia coli
    • Wu, J., and Kaback, H. R. (1996) A general method for determining helix packing in membrane proteins in situ: helices I and II are close to helix VII in the lactose permease of Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 93, 14498-14502.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 14498-14502
    • Wu, J.1    Kaback, H.R.2
  • 35
    • 0031788730 scopus 로고    scopus 로고
    • Human calcitonin receptor is directly targeted to and retained in the basolateral surface of MDCK cells
    • Nussenzveig, D. R., Matos, M. D., and Thaw, C. N. (1998) Human calcitonin receptor is directly targeted to and retained in the basolateral surface of MDCK cells, Am. J. Physiol. 275, C1264-1276.
    • (1998) Am. J. Physiol. , vol.275
    • Nussenzveig, D.R.1    Matos, M.D.2    Thaw, C.N.3
  • 36
    • 0031875263 scopus 로고    scopus 로고
    • Macrophage scavenger receptor confers an adherent phenotype to cells in culture
    • Robbins, A. K., and Horlick, R. A. (1998) Macrophage scavenger receptor confers an adherent phenotype to cells in culture, Biotechniques 25, 240-244.
    • (1998) Biotechniques , vol.25 , pp. 240-244
    • Robbins, A.K.1    Horlick, R.A.2
  • 37
    • 0026496893 scopus 로고
    • Thyrotropin-releasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral peptide binding to G protein-coupled receptors
    • Perlman, J. H., Nussenzveig, D. R., Osman, R., and Gershengorn, M. C. (1992) Thyrotropin-releasing hormone binding to the mouse pituitary receptor does not involve ionic interactions. A model for neutral peptide binding to G protein-coupled receptors, J. Biol. Chem. 267, 24413-24417.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24413-24417
    • Perlman, J.H.1    Nussenzveig, D.R.2    Osman, R.3    Gershengorn, M.C.4
  • 42
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equation of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, J. (1977) Numerical integration of the Cartesian equation of motion of a system with constraints: molecular dynamics of n-alkanes, J. Comput. Phys. 23, 327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, J.3
  • 43
    • 0031909269 scopus 로고    scopus 로고
    • Static and dynamic roles of extracellular loops in G-protein-coupled receptors: A mechanism for sequential binding of thyrotropin-releasing hormone to its receptor
    • Colson, A. O., Perlman, J. H., Smolyar, A., Gershengorn, M. C., and Osman, R. (1998) Static and dynamic roles of extracellular loops in G-protein-coupled receptors: a mechanism for sequential binding of thyrotropin-releasing hormone to its receptor, Biophys. J. 74, 1087-1100.
    • (1998) Biophys. J. , vol.74 , pp. 1087-1100
    • Colson, A.O.1    Perlman, J.H.2    Smolyar, A.3    Gershengorn, M.C.4    Osman, R.5
  • 44
    • 0029953735 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor
    • Perlman, J. H., Laakkonen, L. J., Guarnieri, F., Osman, R., and Gershengorn, M. C. (1996) A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor, Biochemistry 35, 7643-7650.
    • (1996) Biochemistry , vol.35 , pp. 7643-7650
    • Perlman, J.H.1    Laakkonen, L.J.2    Guarnieri, F.3    Osman, R.4    Gershengorn, M.C.5
  • 45
    • 0028020035 scopus 로고
    • Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer
    • Woolf, T. B., and Roux, B. (1994) Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer, Proc. Natl. Acad. Sci. U.S.A. 91, 11631-11635.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11631-11635
    • Woolf, T.B.1    Roux, B.2
  • 46
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B., and Roux, B. (1996) Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer, Proteins 24, 92-114.
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 47
    • 0011613265 scopus 로고    scopus 로고
    • Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane
    • Berneche, S., Nina, M., and Roux, B. (1998) Molecular dynamics simulation of melittin in a dimyristoylphosphatidylcholine bilayer membrane, Biophys. J. 75, 1603-1618.
    • (1998) Biophys. J. , vol.75 , pp. 1603-1618
    • Berneche, S.1    Nina, M.2    Roux, B.3
  • 48
    • 0027515072 scopus 로고
    • Molecular dynamics simulations of a lipid bilayer and of hexadecane: An investigation of membrane fluidity
    • Venable, R. M., Zhang, Y., Hardy, B. J., and Pastor, R. W. (1993) Molecular dynamics simulations of a lipid bilayer and of hexadecane: an investigation of membrane fluidity, Science 262, 223-226.
    • (1993) Science , vol.262 , pp. 223-226
    • Venable, R.M.1    Zhang, Y.2    Hardy, B.J.3    Pastor, R.W.4
  • 49
    • 0032784721 scopus 로고    scopus 로고
    • Lipid lateral diffusion in dilauroylphosphatidylcholine/cholesterol mixed monolayers at the air/water interface
    • Tanaka, K., Manning, P. A., Lau, V. K., and Yu, H. (1999) Lipid Lateral Diffusion in Dilauroylphosphatidylcholine/Cholesterol Mixed Monolayers at the Air/Water Interface, Langmuir 15, 600-606.
    • (1999) Langmuir , vol.15 , pp. 600-606
    • Tanaka, K.1    Manning, P.A.2    Lau, V.K.3    Yu, H.4
  • 50
    • 0029894113 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Novel mixed mode Monte Carlo/stochastic dynamics simulations of the complex between TRH and TRH receptor
    • Laakkonen, L. J., Guarnieri, F., Perlman, J. H., Gershengorn, M. C., and Osman, R. (1996) A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Novel mixed mode Monte Carlo/stochastic dynamics simulations of the complex between TRH and TRH receptor, Biochemistry 35, 7651 -7663.
    • (1996) Biochemistry , vol.35 , pp. 7651-7663
    • Laakkonen, L.J.1    Guarnieri, F.2    Perlman, J.H.3    Gershengorn, M.C.4    Osman, R.5
  • 51
    • 0037062583 scopus 로고    scopus 로고
    • Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin
    • Choi, G., Landin, J., Galan, J. F., Birge, R. R., Albert, A. D., and Yeagle, P. L. (2002) Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin, Biochemistry 41, 7318-7324.
    • (2002) Biochemistry , vol.41 , pp. 7318-7324
    • Choi, G.1    Landin, J.2    Galan, J.F.3    Birge, R.R.4    Albert, A.D.5    Yeagle, P.L.6
  • 52
    • 0036930078 scopus 로고    scopus 로고
    • Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin
    • Saam, J., Tajkhorshid, E., Hayashi, S., and Schulten, K. (2002) Molecular dynamics investigation of primary photoinduced events in the activation of rhodopsin, Biophys. J. 83, 3097-3112.
    • (2002) Biophys. J. , vol.83 , pp. 3097-3112
    • Saam, J.1    Tajkhorshid, E.2    Hayashi, S.3    Schulten, K.4
  • 53
    • 0035498860 scopus 로고    scopus 로고
    • Energetics of ion conduction through the K+ channel
    • Berneche, S., and Roux, B. (2001) Energetics of ion conduction through the K+ channel, Nature 414, 73-77.
    • (2001) Nature , vol.414 , pp. 73-77
    • Berneche, S.1    Roux, B.2
  • 54
    • 0030922145 scopus 로고    scopus 로고
    • Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor
    • Perlman, J. H., Colson, A. O., Wang, W., Bence, K., Osman, R., and Gershengorn, M. C. (1997) Interactions between conserved residues in transmembrane helices 1, 2, and 7 of the thyrotropin-releasing hormone receptor, J. Biol. Chem. 272, 11937-11942.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11937-11942
    • Perlman, J.H.1    Colson, A.O.2    Wang, W.3    Bence, K.4    Osman, R.5    Gershengorn, M.C.6
  • 55
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: What does the rhodopsin structure tell us?
    • Meng, E. C., and Bourne, H. R. (2001) Receptor activation: what does the rhodopsin structure tell us? Trends Pharmacol. Sci. 22, 587-593.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 56
    • 0026489631 scopus 로고
    • Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping
    • Careaga, C. L., and Falke, J. J. (1992) Thermal motions of surface alpha-helices in the D-galactose chemosensory receptor. Detection by disulfide trapping. J. Mol. Biol. 226, 1219-1235.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 57
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether, U. (2000) Uncovering molecular mechanisms involved in activation of G protein-coupled receptors, Endocr. Rev. 21, 90-113.
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 58
    • 0033613232 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase
    • Cai, K., Klein-Seetharaman, J., Hwa, J., Hubbell, W. L., and Khorana, H. G. (1999) Structure and function in rhodopsin: effects of disulfide cross-links in the cytoplasmic face of rhodopsin on transducin activation and phosphorylation by rhodopsin kinase, Biochemistry 38, 12893-12898.
    • (1999) Biochemistry , vol.38 , pp. 12893-12898
    • Cai, K.1    Klein-Seetharaman, J.2    Hwa, J.3    Hubbell, W.L.4    Khorana, H.G.5
  • 60
    • 0037015153 scopus 로고    scopus 로고
    • Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations
    • Rohrig, U. F., Guidoni, L., and Rothlisberger, U. (2002) Early steps of the intramolecular signal transduction in rhodopsin explored by molecular dynamics simulations, Biochemistry 41, 10799-10809.
    • (2002) Biochemistry , vol.41 , pp. 10799-10809
    • Rohrig, U.F.1    Guidoni, L.2    Rothlisberger, U.3
  • 61
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein coupled receptors
    • Ballesteros, J., and Weinstein, H. (1995) Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G protein coupled receptors, Methods Neurosci. 25, 366-428.
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.1    Weinstein, H.2
  • 62
    • 3042663287 scopus 로고    scopus 로고
    • G protein-coupled receptor dimerization: Function and ligand pharmacology
    • Milligan, G. (2004) G protein-coupled receptor dimerization: function and ligand pharmacology, Mol. Pharmacol. 66, 1-7.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1-7
    • Milligan, G.1
  • 63
    • 0035918215 scopus 로고    scopus 로고
    • Constitutive and agonist-dependent homooligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer
    • Kroeger, K. M., Hanyaloglu, A. C., Seeber, R. M., Miles, L. E., and Eidne, K. A. (2001) Constitutive and agonist-dependent homooligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer, J. Biol. Chem. 276, 12736-12743.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12736-12743
    • Kroeger, K.M.1    Hanyaloglu, A.C.2    Seeber, R.M.3    Miles, L.E.4    Eidne, K.A.5
  • 64
    • 0037008771 scopus 로고    scopus 로고
    • Dimerization and phosphorylation of thyrotropin-releasing hormone receptors are modulated by agonist stimulation
    • Zhu, C. C., Cook, L. B., and Hinkle, P. M. (2002) Dimerization and phosphorylation of thyrotropin-releasing hormone receptors are modulated by agonist stimulation, J. Biol. Chem. 277, 28228-28237.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28228-28237
    • Zhu, C.C.1    Cook, L.B.2    Hinkle, P.M.3
  • 65
    • 0035951062 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1
    • Altenbach, C., Klein-Seetharaman, J., Cai, K., Khorana, H. G., and Hubbell, W. L. (2001) Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 316 in helix 8 and residues in the sequence 60-75, covering the cytoplasmic end of helices TM1 and TM2 and their connection loop CL1, Biochemistry 40, 15493-15500.
    • (2001) Biochemistry , vol.40 , pp. 15493-15500
    • Altenbach, C.1    Klein-Seetharaman, J.2    Cai, K.3    Khorana, H.G.4    Hubbell, W.L.5
  • 66
    • 0042165824 scopus 로고    scopus 로고
    • Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor
    • Nikiforovich, G. V., and Marshall, G. R. (2003) Three-dimensional model for meta-II rhodopsin, an activated G-protein-coupled receptor, Biochemistry 42, 9110-9120.
    • (2003) Biochemistry , vol.42 , pp. 9110-9120
    • Nikiforovich, G.V.1    Marshall, G.R.2
  • 67
    • 0035932989 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor
    • Ghanouni, P., Steenhuis, J. J., Farrens, D. L., and Kobilka, B. K. (2001) Agonist-induced conformational changes in the G-protein-coupling domain of the beta 2 adrenergic receptor, Proc. Natl. Acad. Sci. U.S.A. 98, 5997-6002.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5997-6002
    • Ghanouni, P.1    Steenhuis, J.J.2    Farrens, D.L.3    Kobilka, B.K.4
  • 68
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada, T., Ernst, O. P., Palczewski, K., and Hofmann, K. P. (2001) Activation of rhodopsin: new insights from structural and biochemical studies, Trends Biochem. Sci. 26, 318-324.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.