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Volumn 22, Issue 11, 2001, Pages 587-593

Receptor activation: What does the rhodopsin structure tell us?

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; HORMONE DERIVATIVE; NEUROTRANSMITTER; REAGENT; RHODOPSIN;

EID: 0035498937     PISSN: 01656147     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-6147(00)01825-3     Document Type: Review
Times cited : (171)

References (49)
  • 1
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 3
    • 0030775615 scopus 로고    scopus 로고
    • Arrangement of rhodopsin transmembrane α-helices
    • (1997) Nature , vol.389 , pp. 203-206
    • Unger, V.M.1
  • 4
    • 0031565726 scopus 로고    scopus 로고
    • An α-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors
    • (1997) J. Mol. Biol. , vol.272 , pp. 144-164
    • Baldwin, J.M.1
  • 5
    • 0030998038 scopus 로고    scopus 로고
    • The transmembrane 7-α-bundle of rhodopsin: Distance geometry calculations with hydrogen bonding constraints
    • (1997) Biophys. J. , vol.72 , pp. 1963-1985
    • Pogozheva, I.D.1
  • 6
    • 0032575763 scopus 로고    scopus 로고
    • Combined biophysical and biochemical information confirms arrangement of transmembrane helices visible from the three-dimensional map of frog rhodopsin
    • (1998) J. Mol. Biol. , vol.281 , pp. 741-754
    • Herzyk, P.1    Hubbard, R.E.2
  • 8
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1
  • 9
    • 0034705612 scopus 로고    scopus 로고
    • Movement of retinal along the visual transduction path
    • (2000) Science , vol.288 , pp. 2209-2212
    • Borhan, B.1
  • 11
  • 12
    • 0028105203 scopus 로고
    • The location of the chromophore in rhodopsin: A photoaffinity study
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10165-10173
    • Zhang, H.1
  • 13
    • 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
    • (1999) Biochemistry , vol.38 , pp. 12893-12898
    • Cai, K.1
  • 14
    • 0033554440 scopus 로고    scopus 로고
    • Tertiary interactions between transmembrane segments 3 and 5 near the cytoplasmic side of rhodopsin
    • (1999) Biochemistry , vol.38 , pp. 12033-12040
    • Yu, H.1    Oprian, D.D.2
  • 15
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metal-ion-binding sites linking transmembrane helices C and F
    • (1996) Nature , vol.383 , pp. 347-350
    • Sheikh, S.P.1
  • 17
    • 0031473727 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Topology of the C-terminal polypeptide chain in relation to the cytoplasmic loops
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 14267-14272
    • Cai, K.1
  • 18
    • 0033580636 scopus 로고    scopus 로고
    • Tertiary interactions between the fifth and sixth transmembrane segments of rhodopsin
    • (1999) Biochemistry , vol.38 , pp. 6597-6603
    • Struthers, M.1
  • 19
    • 0034636820 scopus 로고    scopus 로고
    • G protein-coupled receptor activation: Analysis of a highly constrained, 'straitjacketed' rhodopsin
    • (2000) Biochemistry , vol.39 , pp. 7938-7942
    • Struthers, M.1
  • 20
    • 0028822684 scopus 로고
    • A general method for mapping tertiary contacts between amino acid residues in membrane-embedded proteins
    • (1995) Biochemistry , vol.34 , pp. 14963-14969
    • Yu, H.1
  • 21
    • 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
    • (1996) Biochemistry , vol.35 , pp. 14040-14046
    • Yang, K.1
  • 22
    • 0033554396 scopus 로고    scopus 로고
    • State-dependent disulfide cross-linking in rhodopsin
    • (1999) Biochemistry , vol.38 , pp. 12028-12032
    • Yu, H.1
  • 24
    • 0030975286 scopus 로고    scopus 로고
    • Transducin-α C-terminal peptide binding site consists of C-D and E-F loops of rhodopsin
    • (1997) J. Biol. Chem. , vol.272 , pp. 6519-6524
    • Acharya, S.1
  • 25
    • 0034695476 scopus 로고    scopus 로고
    • The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction
    • (2000) J. Biol. Chem. , vol.275 , pp. 1930-1936
    • Marin, E.P.1
  • 27
    • 0026489631 scopus 로고
    • Thermal motions of surface α-helices in the d-galactose chemosensory receptor. Detection by disulfide trapping
    • (1992) J. Mol. Biol. , vol.226 , pp. 1219-1235
    • Careaga, C.L.1    Falke, J.J.2
  • 28
    • 0027443076 scopus 로고
    • Formation of the meta II photointermediate is accompanied by conformational changes in the cytoplasmic surface of rhodopsin
    • (1993) Biochemistry , vol.32 , pp. 12025-12032
    • Resek, J.F.1
  • 29
    • 0033594869 scopus 로고    scopus 로고
    • Single-cysteine substitution mutants at amino acid positions 55-75, the sequence connecting the cytoplasmic ends of helices I and II in rhodopsin: Reactivity of the sulfhydryl groups and their derivatives identifies a tertiary structure that changes upon light-activation
    • (1999) Biochemistry , vol.38 , pp. 7938-7944
    • Klein-Seetharaman, J.1
  • 30
    • 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
    • (1995) Biochemistry , vol.34 , pp. 8812-8819
    • Farahbakhsh, Z.T.1
  • 31
    • 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
    • (1996) Biochemistry , vol.35 , pp. 12470-12478
    • Altenbach, C.1
  • 32
    • 0033594926 scopus 로고    scopus 로고
    • Structural features of the C-terminal domain of bovine rhodopsin: A site-directed spin-labeling study
    • (1999) Biochemistry , vol.38 , pp. 7918-7924
    • Langen, R.1
  • 33
    • 0033594988 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the sequence 306-322 extending from helix VII to the palmitoylation sites in rhodopsin: A site-directed spin-labeling study
    • (1999) Biochemistry , vol.38 , pp. 7931-7937
    • Altenbach, C.1
  • 34
    • 0033594981 scopus 로고    scopus 로고
    • Structural features and light-dependent changes in the sequence 59-75 connecting helices I and II in rhodopsin: A site-directed spin-labeling study
    • (1999) Biochemistry , vol.38 , pp. 7945-7949
    • Altenbach, C.1
  • 35
    • 0033594866 scopus 로고    scopus 로고
    • Single-cysteine substitution mutants at amino acid positions 306-321 in rhodopsin, the sequence between the cytoplasmic end of helix VII and the palmitoylation sites: Sulfhydryl reactivity and transducin activation reveal a tertiary structure
    • (1999) Biochemistry , vol.38 , pp. 7925-7930
    • Cai, K.1
  • 36
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy
    • (1999) J. Biol. Chem. , vol.274 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 37
    • 0029818639 scopus 로고    scopus 로고
    • Structure and function in rhodopsin. Single cysteine substitution mutants in the cytoplasmic interhelical E-F loop region show position-specific effects in transducin activation
    • (1996) Biochemistry , vol.35 , pp. 12464-12469
    • Yang, K.1
  • 40
    • 0033546197 scopus 로고    scopus 로고
    • Similar structures and shared switch mechanisms of the β2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation
    • (1999) J. Biol. Chem. , vol.274 , pp. 17033-17041
    • Sheikh, S.P.1
  • 42
    • 0033944938 scopus 로고    scopus 로고
    • Partial agonism through a zinc-ion switch constructed between transmembrane domains III and VII in the tachykinin NK(1) receptor
    • (2000) Mol. Pharmacol. , vol.58 , pp. 263-270
    • Holst, B.1
  • 43
    • 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)
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1
  • 45
  • 46
    • 0033025734 scopus 로고    scopus 로고
    • C5a receptor activation. Genetic identification of critical residues in four transmembrane helices
    • (1999) J. Biol. Chem. , vol.274 , pp. 15757-15765
    • Baranski, T.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.