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Volumn 8, Issue 367, 2015, Pages

Conformational activation of visual rhodopsin in native disc membranes

Author keywords

[No Author keywords available]

Indexed keywords

RHODOPSIN;

EID: 84938355875     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2005646     Document Type: Article
Times cited : (34)

References (64)
  • 1
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • R. Fredriksson, M. C. Lagerström, L. G. Lundin, H. B. Schiöth, The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol. Pharmacol. 63, 1256-1272 (2003).
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerström, M.C.2    Lundin, L.G.3    Schiöth, H.B.4
  • 2
    • 77952906089 scopus 로고    scopus 로고
    • Structure and activation of the visual pigment rhodopsin
    • S. O. Smith, Structure and activation of the visual pigment rhodopsin. Annu. Rev. Biophys. 39, 309-328 (2010).
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 309-328
    • Smith, S.O.1
  • 4
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • D. L. Farrens, C. Altenbach, K. Yang, W. L. Hubbell, H. G. Khorana, Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 274, 768-770 (1996).
    • (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
  • 5
    • 44949236117 scopus 로고    scopus 로고
    • High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation
    • C. Altenbach, A. K. Kusnetzow, O. P. Ernst, K. P. Hofmann, W. L. Hubbell, High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation. Proc. Natl. Acad. Sci. U.S.A. 105, 7439-7444 (2008).
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7439-7444
    • Altenbach, C.1    Kusnetzow, A.K.2    Ernst, O.P.3    Hofmann, K.P.4    Hubbell, W.L.5
  • 6
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin - Movement of helix F detected by site-specific chemical labeling and fluorescence spectroscopy
    • T. D. Dunham, D. L. Farrens, Conformational changes in rhodopsin - Movement of helix F detected by site-specific chemical labeling and fluorescence spectroscopy. J. Biol. Chem. 274, 1683-1690 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 7
    • 68949143130 scopus 로고    scopus 로고
    • The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins
    • H. Tsukamoto, D. L. Farrens, M. Koyanagi, A. Terakita, The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins. J. Biol. Chem. 284, 20676-20683 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 20676-20683
    • Tsukamoto, H.1    Farrens, D.L.2    Koyanagi, M.3    Terakita, A.4
  • 8
    • 77951877209 scopus 로고    scopus 로고
    • Tracking G-protein-coupled receptor activation using genetically encoded infrared probes
    • S. Ye, E. Zaitseva, G. Caltabiano, G. F. X. Schertler, T. P. Sakmar, X. Deupi, R. Vogel, Tracking G-protein-coupled receptor activation using genetically encoded infrared probes. Nature 464, 1386-1389 (2010).
    • (2010) Nature , vol.464 , pp. 1386-1389
    • Ye, S.1    Zaitseva, E.2    Caltabiano, G.3    Schertler, G.F.X.4    Sakmar, T.P.5    Deupi, X.6    Vogel, R.7
  • 11
    • 0037062583 scopus 로고    scopus 로고
    • Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin
    • G. Choi, J. Landin, J. F. Galan, R. R. Birge, A. D. Albert, P. L. Yeagle, Structural studies of metarhodopsin II, the activated form of the G-protein coupled receptor, rhodopsin. Biochemistry 41, 7318-7324 (2002).
    • (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
  • 12
    • 33746321096 scopus 로고    scopus 로고
    • Crystallographic analysis of primary visual photochemistry
    • H. Nakamichi, T. Okada, Crystallographic analysis of primary visual photochemistry. Angew. Chem. Int. Ed. Engl. 45, 4270-4273 (2006).
    • (2006) Angew. Chem. Int. Ed. Engl. , vol.45 , pp. 4270-4273
    • Nakamichi, H.1    Okada, T.2
  • 13
    • 33748079137 scopus 로고    scopus 로고
    • Local peptide movement in the photoreaction intermediate of rhodopsin
    • H. Nakamichi, T. Okada, Local peptide movement in the photoreaction intermediate of rhodopsin. Proc. Natl. Acad. Sci. U.S.A. 103, 12729-12734 (2006).
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 12729-12734
    • Nakamichi, H.1    Okada, T.2
  • 15
    • 34250340151 scopus 로고    scopus 로고
    • Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography
    • H. Nakamichi, V. Buss, T. Okada, Photoisomerization mechanism of rhodopsin and 9-cis-rhodopsin revealed by x-ray crystallography. Biophys. J. 92, L106-L108 (2007).
    • (2007) Biophys. J. , vol.92 , pp. L106-L108
    • Nakamichi, H.1    Buss, V.2    Okada, T.3
  • 16
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • J. H. Park, P. Scheerer, K. P. Hofmann, H. W. Choe, O. P. Ernst, Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454, 183-187 (2008).
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 25
    • 70349679105 scopus 로고    scopus 로고
    • Protein tertiary structural changes visualized by time-resolved x-ray solution scattering
    • S. Ahn, K. H. Kim, Y. Kim, J. Kim, H. Ihee, Protein tertiary structural changes visualized by time-resolved x-ray solution scattering. J. Phys. Chem. B 113, 13131-13133 (2009).
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13131-13133
    • Ahn, S.1    Kim, K.H.2    Kim, Y.3    Kim, J.4    Ihee, H.5
  • 28
    • 78649811402 scopus 로고    scopus 로고
    • Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond x-ray solution scattering
    • K. H. Kim, K. Y. Oang, J. Kim, J. H. Lee, Y. Kim, H. Ihee, Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond x-ray solution scattering. Chem. Commun. 47, 289-291 (2011).
    • (2011) Chem. Commun. , vol.47 , pp. 289-291
    • Kim, K.H.1    Oang, K.Y.2    Kim, J.3    Lee, J.H.4    Kim, Y.5    Ihee, H.6
  • 36
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • E. R. Henry, J. Hofrichter, Singular value decomposition: Application to analysis of experimental data. Methods Enzymol. 210, 129-192 (1992).
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 37
    • 0035498356 scopus 로고    scopus 로고
    • Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: Possible coupling to proton uptake and formation of the active form of meta II
    • O. Kuwata, C. Yuan, S. Misra, R. Govindjee, T. G. Ebrey, Kinetics and pH dependence of light-induced deprotonation of the Schiff base of rhodopsin: Possible coupling to proton uptake and formation of the active form of meta II. Biochemistry 66, 1283-1299 (2001).
    • (2001) Biochemistry , vol.66 , pp. 1283-1299
    • Kuwata, O.1    Yuan, C.2    Misra, S.3    Govindjee, R.4    Ebrey, T.G.5
  • 38
    • 55249090879 scopus 로고    scopus 로고
    • Monitoring the conformational changes of photoactivated rhodopsin from microseconds to seconds by transient fluorescence spectroscopy
    • D. Hoersch, H. Otto, I. Wallat, M. P. Heyn, Monitoring the conformational changes of photoactivated rhodopsin from microseconds to seconds by transient fluorescence spectroscopy. Biochemistry 47, 11518-11527 (2008).
    • (2008) Biochemistry , vol.47 , pp. 11518-11527
    • Hoersch, D.1    Otto, H.2    Wallat, I.3    Heyn, M.P.4
  • 39
    • 0028957661 scopus 로고
    • Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy
    • D. L. Farrens, H. G. Khorana, Structure and function in rhodopsin. Measurement of the rate of metarhodopsin II decay by fluorescence spectroscopy. J. Biol. Chem. 270, 5073-5076 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 5073-5076
    • Farrens, D.L.1    Khorana, H.G.2
  • 40
    • 0035797877 scopus 로고    scopus 로고
    • Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms
    • P. L. Yeagle, G. Choi, A. D. Albert, Studies on the structure of the G-protein-coupled receptor rhodopsin including the putative G-protein binding site in unactivated and activated forms. Biochemistry 40, 11932-11937 (2001).
    • (2001) Biochemistry , vol.40 , pp. 11932-11937
    • Yeagle, P.L.1    Choi, G.2    Albert, A.D.3
  • 41
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs)
    • D. C. Teller, T. Okada, C. A. Behnke, K. Palczewski, R. E. Stenkamp, Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-protein-coupled receptors (GPCRs). Biochemistry 40, 7761-7772 (2001).
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 43
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
    • T. Okada, M. Sugihara, A. N. Bondar, M. Elstner, P. Entel, V. Buss, The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure. J. Mol. Biol. 342, 571-583 (2004).
    • (2004) J. Mol. Biol. , vol.342 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 46
    • 47749095553 scopus 로고    scopus 로고
    • Alternative models for two crystal structures of bovine rhodopsin
    • R. E. Stenkamp, Alternative models for two crystal structures of bovine rhodopsin. Acta Crystallogr. D Biol. Crystallogr. D64, 902-904 (2008).
    • (2008) Acta Crystallogr. D Biol. Crystallogr. , vol.D64 , pp. 902-904
    • Stenkamp, R.E.1
  • 48
    • 0036008503 scopus 로고    scopus 로고
    • A genetic algorithm for the identification of conformationally invariant regions in protein molecules
    • T. R. Schneider, A genetic algorithm for the identification of conformationally invariant regions in protein molecules. Acta Crystallogr. D Biol. Crystallogr. 58, 195-208 (2002).
    • (2002) Acta Crystallogr. D Biol. Crystallogr. , vol.58 , pp. 195-208
    • Schneider, T.R.1
  • 50
    • 0038159530 scopus 로고    scopus 로고
    • Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes
    • Y. Liang, D. Fotiadis, S. Filipek, D. A. Saperstein, K. Palczewski, A. Engel, Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278, 21655-21662 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 21655-21662
    • Liang, Y.1    Fotiadis, D.2    Filipek, S.3    Saperstein, D.A.4    Palczewski, K.5    Engel, A.6
  • 52
    • 79953225494 scopus 로고    scopus 로고
    • Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis
    • P. J. Cross, R. C. Dobson, M. L. Patchett, E. J. Parker, Tyrosine latching of a regulatory gate affords allosteric control of aromatic amino acid biosynthesis. J. Biol. Chem. 286, 10216-10224 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 10216-10224
    • Cross, P.J.1    Dobson, R.C.2    Patchett, M.L.3    Parker, E.J.4
  • 54
    • 0023110336 scopus 로고
    • Evidence for rhodopsin refolding during the decay of Meta II
    • K. J. Rothschild, J. Gillespie, W. J. DeGrip, Evidence for rhodopsin refolding during the decay of Meta II. Biophys. J. 51, 345-350 (1987).
    • (1987) Biophys. J. , vol.51 , pp. 345-350
    • Rothschild, K.J.1    Gillespie, J.2    DeGrip, W.J.3
  • 55
    • 33646382407 scopus 로고    scopus 로고
    • Conformational states and dynamics of rhodopsin in micelles and bilayers
    • A. K. Kusnetzow, C. Altenbach, W. L. Hubbell, Conformational states and dynamics of rhodopsin in micelles and bilayers. Biochemistry 45, 5538-5550 (2006).
    • (2006) Biochemistry , vol.45 , pp. 5538-5550
    • Kusnetzow, A.K.1    Altenbach, C.2    Hubbell, W.L.3
  • 56
  • 59
    • 0032951553 scopus 로고    scopus 로고
    • Alamethicin helices in a bilayer and in solution: Molecular dynamics simulations
    • D. P. Tieleman, M. S. Sansom, H. J. Berendsen, Alamethicin helices in a bilayer and in solution: Molecular dynamics simulations. Biophys. J. 76, 40-49 (1999).
    • (1999) Biophys. J. , vol.76 , pp. 40-49
    • Tieleman, D.P.1    Sansom, M.S.2    Berendsen, H.J.3
  • 60
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, M. H. J. Koch, CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995).
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.