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Volumn 50, Issue 47, 2011, Pages 10399-10407

Preparation of an activated rhodopsin/transducin complex using a constitutively active mutant of rhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATED COMPLEX; BICELLES; CONSTITUTIVELY ACTIVES; COVALENTLY BOUND; DETERGENT SOLUTION; GUANINE NUCLEOTIDES; IMMUNOAFFINITY CHROMATOGRAPHY; IMMUNOAFFINITY COLUMNS; MOLAR RATIO; SUCROSE DENSITY GRADIENT CENTRIFUGATION; TRANSDUCIN;

EID: 81855226606     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201126r     Document Type: Article
Times cited : (16)

References (58)
  • 2
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum, D. M., Rasmussen, S. G., and Kobilka, B. K. (2009) The structure and function of G-protein-coupled receptors Nature 459, 356-363
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 3
    • 77952906089 scopus 로고    scopus 로고
    • Structure and activation of the visual pigment rhodopsin
    • Smith, S. O. (2010) Structure and activation of the visual pigment rhodopsin Annu. Rev. Biophys. 39, 309-328
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 4
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • Kobilka, B. and Schertler, G. F. (2008) New G-protein-coupled receptor crystal structures: insights and limitations Trends Pharmacol. Sci. 29, 79-83
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.2
  • 8
    • 79959564813 scopus 로고    scopus 로고
    • Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation
    • Lebon, G., Warne, T., Edwards, P. C., Bennett, K., Langmead, C. J., Leslie, A. G., and Tate, C. G. (2011) Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation Nature 474, 521-525
    • (2011) Nature , vol.474 , pp. 521-525
    • Lebon, G.1    Warne, T.2    Edwards, P.C.3    Bennett, K.4    Langmead, C.J.5    Leslie, A.G.6    Tate, C.G.7
  • 9
    • 6344248639 scopus 로고    scopus 로고
    • Structure of bovine rhodopsin in a trigonal crystal form
    • DOI 10.1016/j.jmb.2004.08.090, PII S0022283604010903
    • Li, J., Edwards, P. C., Burghammer, M., Villa, C., and Schertler, G. F. (2004) Structure of bovine rhodopsin in a trigonal crystal form J. Mol. Biol. 343, 1409-1438 (Pubitemid 39387834)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1409-1438
    • Li, J.1    Edwards, P.C.2    Burghammer, M.3    Villa, C.4    Schertler, G.F.X.5
  • 10
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • DOI 10.1038/nature06925, PII NATURE06925
    • Murakami, M. and Kouyama, T. (2008) Crystal structure of squid rhodopsin Nature 453, 363-367 (Pubitemid 351693128)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 11
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • DOI 10.1002/anie.200600595
    • Nakamichi, H. and Okada, T. (2006) Crystallographic analysis of primary visual photochemistry Angew. Chem., Int. Ed. 45, 4270-4273 (Pubitemid 44105630)
    • (2006) Angewandte Chemie - International Edition , vol.45 , Issue.26 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 24
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • DOI 10.1038/nature07063, PII NATURE07063
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin Nature 454, 183-187 (Pubitemid 351969893)
    • (2008) Nature , vol.454 , Issue.7201 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.-W.4    Ernst, O.P.5
  • 27
    • 77953252509 scopus 로고    scopus 로고
    • The quest to understand heterotrimeric G protein signaling
    • Tesmer, J. J. (2010) The quest to understand heterotrimeric G protein signaling Nat. Struct. Mol. Biol. 17, 650-652
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 650-652
    • Tesmer, J.J.1
  • 29
    • 34447509986 scopus 로고    scopus 로고
    • Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins
    • DOI 10.1074/jbc.M701433200
    • Bayburt, T. H., Leitz, A. J., Xie, G., Oprian, D. D., and Sligar, S. G. (2007) Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins J. Biol. Chem. 282, 14875-14881 (Pubitemid 47093370)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14875-14881
    • Bayburt, T.H.1    Leitz, A.J.2    Xie, G.3    Oprian, D.D.4    Sligar, S.G.5
  • 31
    • 67049154294 scopus 로고    scopus 로고
    • Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex
    • Jastrzebska, B., Goc, A., Golczak, M., and Palczewski, K. (2009) Phospholipids are needed for the proper formation, stability, and function of the photoactivated rhodopsin-transducin complex Biochemistry 48, 5159-5170
    • (2009) Biochemistry , vol.48 , pp. 5159-5170
    • Jastrzebska, B.1    Goc, A.2    Golczak, M.3    Palczewski, K.4
  • 32
    • 59649125366 scopus 로고    scopus 로고
    • Isolation and functional characterization of a stable complex between photoactivated rhodopsin and the G protein, transducin
    • Jastrzebska, B., Golczak, M., Fotiadis, D., Engel, A., and Palczewski, K. (2009) Isolation and functional characterization of a stable complex between photoactivated rhodopsin and the G protein, transducin FASEB J. 23, 371-381
    • (2009) FASEB J. , vol.23 , pp. 371-381
    • Jastrzebska, B.1    Golczak, M.2    Fotiadis, D.3    Engel, A.4    Palczewski, K.5
  • 33
    • 77953384365 scopus 로고    scopus 로고
    • Complexes between photoactivated rhodopsin and transducin: Progress and questions
    • Jastrzebska, B., Tsybovsky, Y., and Palczewski, K. (2010) Complexes between photoactivated rhodopsin and transducin: progress and questions Biochem. J. 428, 1-10
    • (2010) Biochem. J. , vol.428 , pp. 1-10
    • Jastrzebska, B.1    Tsybovsky, Y.2    Palczewski, K.3
  • 35
    • 44649152217 scopus 로고    scopus 로고
    • Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin
    • Standfuss, J., Zaitseva, E., Mahalingam, M., and Vogel, R. (2008) Structural impact of the E113Q counterion mutation on the activation and deactivation pathways of the G protein-coupled receptor rhodopsin J. Mol. Biol. 380, 145-157
    • (2008) J. Mol. Biol. , vol.380 , pp. 145-157
    • Standfuss, J.1    Zaitseva, E.2    Mahalingam, M.3    Vogel, R.4
  • 37
    • 0037465339 scopus 로고    scopus 로고
    • An opsin mutant with increased thermal stability
    • DOI 10.1021/bi020611z
    • Xie, G., Gross, A. K., and Oprian, D. D. (2003) An opsin mutant with increased thermal stability Biochemistry 42, 1995-2001 (Pubitemid 36258672)
    • (2003) Biochemistry , vol.42 , Issue.7 , pp. 1995-2001
    • Xie, G.1    Gross, A.K.2    Oprian, D.D.3
  • 41
    • 0021766626 scopus 로고
    • Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides
    • MacKenzie, D., Arendt, A., Hargrave, P., McDowell, J. H., and Molday, R. S. (1984) Localization of binding sites for carboxyl terminal specific anti-rhodopsin monoclonal antibodies using synthetic peptides Biochemistry 23, 6544-6549
    • (1984) Biochemistry , vol.23 , pp. 6544-6549
    • MacKenzie, D.1    Arendt, A.2    Hargrave, P.3    McDowell, J.H.4    Molday, R.S.5
  • 42
    • 0020713543 scopus 로고
    • Monoclonal antibodies to rhodopsin: Characterization, cross-reactivity, and application as structural probes
    • Molday, R. S. and MacKenzie, D. (1983) Monoclonal antibodies to rhodopsin: characterization, cross-reactivity, and application as structural probes Biochemistry 22, 653-660
    • (1983) Biochemistry , vol.22 , pp. 653-660
    • Molday, R.S.1    MacKenzie, D.2
  • 43
    • 0023654299 scopus 로고
    • Allosteric behavior in transducin activation mediated by rhodopsin. Initial rate analysis of guanine nucleotide exchange
    • Wessling-Resnick, M. and Johnson, G. L. (1987) Allosteric behavior in transducin activation mediated by rhodopsin. Initial rate analysis of guanine nucleotide exchange J. Biol. Chem. 262, 3697-3705
    • (1987) J. Biol. Chem. , vol.262 , pp. 3697-3705
    • Wessling-Resnick, M.1    Johnson, G.L.2
  • 45
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • DOI 10.1073/pnas.212519299
    • Reeves, P. J., Callewaert, N., Contreras, R., and Khorana, H. G. (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line Proc. Natl. Acad. Sci. U. S. A. 99, 13419-13424 (Pubitemid 35215396)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.21 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 46
    • 0025757195 scopus 로고
    • Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore
    • Zhukovsky, E. A., Robinson, P. R., and Oprian, D. D. (1991) Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore Science 251, 558-560 (Pubitemid 21926157)
    • (1991) Science , vol.251 , Issue.4993 , pp. 558-560
    • Zhukovsky, E.A.1    Robinson, P.R.2    Oprian, D.D.3
  • 47
    • 0033533398 scopus 로고    scopus 로고
    • Spectral tuning in the human blue cone pigment
    • Fasick, J. I., Lee, N., and Oprian, D. D. (1999) Spectral tuning in the human blue cone pigment Biochemistry 38, 11593-11596
    • (1999) Biochemistry , vol.38 , pp. 11593-11596
    • Fasick, J.I.1    Lee, N.2    Oprian, D.D.3
  • 48
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6, 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 49
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 50
    • 0021923172 scopus 로고
    • Inhibition of monoclonal antibody binding and proteolysis by light-induced phosphorylation of rhodopsin
    • DOI 10.1021/bi00324a036
    • Molday, R. S. and MacKenzie, D. (1985) Inhibition of monoclonal antibody binding and proteolysis by light-induced phosphorylation of rhodopsin Biochemistry 24, 776-781 (Pubitemid 15142260)
    • (1985) Biochemistry , vol.24 , Issue.3 , pp. 776-781
    • Molday, R.S.1    MacKenzie, D.2
  • 51
    • 0020488317 scopus 로고
    • Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium
    • Emeis, D., Kuhn, H., Reichert, J., and Hofmann, K. P. (1982) Complex formation between metarhodopsin II and GTP-binding protein in bovine photoreceptor membranes leads to a shift of the photoproduct equilibrium FEBS Lett. 143, 29-34
    • (1982) FEBS Lett. , vol.143 , pp. 29-34
    • Emeis, D.1    Kuhn, H.2    Reichert, J.3    Hofmann, K.P.4
  • 52
    • 0024427734 scopus 로고
    • The transitory complex between photoexcited rhodopsin and transducin. Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin
    • Bornancin, F., Pfister, C., and Chabre, M. (1989) The transitory complex between photoexcited rhodopsin and transducin. Reciprocal interaction between the retinal site in rhodopsin and the nucleotide site in transducin Eur. J. Biochem. 184, 687-698 (Pubitemid 19260698)
    • (1989) European Journal of Biochemistry , vol.184 , Issue.3 , pp. 687-698
    • Bornancin, F.1    Pfister, C.2    Chabre, M.3
  • 54
    • 0001296931 scopus 로고
    • Interactions between Photoexcited Rhodopsin and Light-Activated Enzymes in Rods
    • Kuhn, H. (1984) Interactions Between Photoexcited Rhodopsin and Light-Activated Enzymes in Rods Prog. Retinal Res. 3, 123-156
    • (1984) Prog. Retinal Res. , vol.3 , pp. 123-156
    • Kuhn, H.1
  • 55
    • 40849130624 scopus 로고    scopus 로고
    • Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles
    • Banerjee, S., Huber, T., and Sakmar, T. P. (2008) Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles J. Mol. Biol. 377, 1067-1081
    • (2008) J. Mol. Biol. , vol.377 , pp. 1067-1081
    • Banerjee, S.1    Huber, T.2    Sakmar, T.P.3
  • 57
    • 0024362631 scopus 로고
    • Effect of carboxylic acid side chains on the absorption maximum of visual pigments
    • Zhukovsky, E. A. and Oprian, D. D. (1989) Effect of carboxylic acid side chains on the absorption maximum of visual pigments Science 246, 928-930 (Pubitemid 20010506)
    • (1989) Science , vol.246 , Issue.4932 , pp. 928-930
    • Zhukovsky, E.A.1    Oprian, D.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.