메뉴 건너뛰기




Volumn 44, Issue 24, 2005, Pages 8757-8769

Cysteine residues in the human cannabinoid receptor: Only C257 and C264 are required for a functional receptor, and steric bulk at C386 impairs antagonist SR141716A binding

Author keywords

[No Author keywords available]

Indexed keywords

BRAIN; CELL MEMBRANES; METHANE; MUTAGENESIS; NEUROLOGY; SULFUR COMPOUNDS;

EID: 20544465661     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0472651     Document Type: Article
Times cited : (51)

References (83)
  • 1
    • 0042991377 scopus 로고    scopus 로고
    • Pharmacophores for ligand recognition and activation/inactivation of the cannabinoid receptors
    • Reggio, P. H. (2003) Pharmacophores for ligand recognition and activation/inactivation of the cannabinoid receptors. Curr. Pharm. Des. 9, 1607-1633.
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 1607-1633
    • Reggio, P.H.1
  • 3
    • 0035053627 scopus 로고    scopus 로고
    • Retrograde inhibition of presynaptic calcium influx by endogenous cannabinoids at excitatory synapses onto Purkinje cells
    • Kreitzer, A. C., and Regehr, W. G. (2001) Retrograde inhibition of presynaptic calcium influx by endogenous cannabinoids at excitatory synapses onto Purkinje cells, Neuron 29, 717-727.
    • (2001) Neuron , vol.29 , pp. 717-727
    • Kreitzer, A.C.1    Regehr, W.G.2
  • 4
    • 0035967145 scopus 로고    scopus 로고
    • Endogenous cannabinoids mediate retrograde signalling at hippocampal synapses
    • Wilson, R. I., and Nicoll, R. A. (2001) Endogenous cannabinoids mediate retrograde signalling at hippocampal synapses. Nature 410, 588-592.
    • (2001) Nature , vol.410 , pp. 588-592
    • Wilson, R.I.1    Nicoll, R.A.2
  • 5
    • 0035050883 scopus 로고    scopus 로고
    • Endogenous cannabinoids mediate retrograde signals from depolarized postsynaptic neurons to presynaptic terminals
    • Ohno-Shosaku, T., Maejima, T., and Kano, M. (2001) Endogenous cannabinoids mediate retrograde signals from depolarized postsynaptic neurons to presynaptic terminals, Neuron 29, 729-738.
    • (2001) Neuron , vol.29 , pp. 729-738
    • Ohno-Shosaku, T.1    Maejima, T.2    Kano, M.3
  • 6
    • 0029904838 scopus 로고    scopus 로고
    • Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
    • Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., and Gilula, N. B. (1996) Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides, Nature 384, 83-87.
    • (1996) Nature , vol.384 , pp. 83-87
    • Cravatt, B.F.1    Giang, D.K.2    Mayfield, S.P.3    Boger, D.L.4    Lerner, R.A.5    Gilula, N.B.6
  • 8
    • 0030870722 scopus 로고    scopus 로고
    • A second endogenous cannabinoid that modulates long-term potentiation
    • Stella, N., Schweitzer, P., and Piomelli, D. (1997) A second endogenous cannabinoid that modulates long-term potentiation, Nature 388, 773-778.
    • (1997) Nature , vol.388 , pp. 773-778
    • Stella, N.1    Schweitzer, P.2    Piomelli, D.3
  • 9
    • 0041854348 scopus 로고    scopus 로고
    • Membrane assembly of the cannabinoid receptor 1: Impact of a long N-terminal tail
    • Andersson, H., D'Antona, A. M., Kendall, D. A., Von Heijne, G., and Chin, C. N. (2003) Membrane assembly of the cannabinoid receptor 1: Impact of a long N-terminal tail, Mol. Pharmacol. 64, 570-577.
    • (2003) Mol. Pharmacol. , vol.64 , pp. 570-577
    • Andersson, H.1    D'Antona, A.M.2    Kendall, D.A.3    Von Heijne, G.4    Chin, C.N.5
  • 10
    • 0037716778 scopus 로고    scopus 로고
    • Integrity of extracellular loop 1 of the human cannabinoid receptor 1 is critical for high-affinity binding of the ligand CP 55,940 but not SR 141716A
    • Murphy, J. W., and Kendall, D. A. (2003) Integrity of extracellular loop 1 of the human cannabinoid receptor 1 is critical for high-affinity binding of the ligand CP 55,940 but not SR 141716A, Biochem. Pharmacol. 65, 1623-1631.
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 1623-1631
    • Murphy, J.W.1    Kendall, D.A.2
  • 11
    • 0036892304 scopus 로고    scopus 로고
    • N-(Piperidin-1-yl)-5-(4-chlorophenyl)-1-(2,4-dichorophenyl) -4-methyl-1H-pyrazole-3-carboxamide (SR141716A) interaction with LYS 3.28(192) is crucial for its inverse agonism at the cannabinoid CB1 receptor
    • Hurst, D. P., Lynch, D. L., Barnett-Norris, J., Hyatt, S. M., Seltzman. H. H., Zhong, M., Song, Z. H., Nie, J., Lewis, D., and Reggio, P. H. (2002) N-(Piperidin-1-yl)-5-(4-chlorophenyl)-1-(2,4-dichorophenyl)-4-methyl-1H- pyrazole-3-carboxamide (SR141716A) interaction with LYS 3.28(192) is crucial for its inverse agonism at the cannabinoid CB1 receptor. Mol. Pharmacol. 62, 1274-1287.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 1274-1287
    • Hurst, D.P.1    Lynch, D.L.2    Barnett-Norris, J.3    Hyatt, S.M.4    Seltzman, H.H.5    Zhong, M.6    Song, Z.H.7    Nie, J.8    Lewis, D.9    Reggio, P.H.10
  • 13
    • 0025085912 scopus 로고
    • Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187
    • Karnik, S. S., and Khorana, H. G. (1990) Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187, J. Biol. Chem. 265, 17520-17524.
    • (1990) J. Biol. Chem. , vol.265 , pp. 17520-17524
    • Karnik, S.S.1    Khorana, H.G.2
  • 14
    • 0028922277 scopus 로고
    • Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons
    • Ridge, K. D., Lu, Z., Liu, X., and Khorana, H. G. (1995) Structure and function in rhodopsin. Separation and characterization of the correctly folded and misfolded opsins produced on expression of an opsin mutant gene containing only the native intradiscal cysteine codons, Biochemistry 34, 3261-3267.
    • (1995) Biochemistry , vol.34 , pp. 3261-3267
    • Ridge, K.D.1    Lu, Z.2    Liu, X.3    Khorana, H.G.4
  • 15
    • 0033515036 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function
    • Hwa, J., Reeves, P. J., Klein-Seetharaman, J., Davidson, F., and Khorana, H. G. (1999) Structure and function in rhodopsin: Further elucidation of the role of the intradiscal cysteines, Cys-110, -185, and -187, in rhodopsin folding and function, Proc. Natl. Acad. Sci. U.S.A. 96, 1932-1935.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1932-1935
    • Hwa, J.1    Reeves, P.J.2    Klein-Seetharaman, J.3    Davidson, F.4    Khorana, H.G.5
  • 16
    • 0035942215 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants
    • Hwa, J., Klein-Seetharaman, J., and Khorana, H. G. (2001) Structure and function in rhodopsin: Mass spectrometric identification of the abnormal intradiscal disulfide bond in misfolded retinitis pigmentosa mutants, Proc. Natl. Acad. Sci. U.S.A. 98, 4872-4876.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4872-4876
    • Hwa, J.1    Klein-Seetharaman, J.2    Khorana, H.G.3
  • 17
    • 0027269816 scopus 로고
    • Roles of sulfhydryl and disulfide groups in the binding of CP-55,940 to rat brain cannabinoid receptor
    • Lu, R., Hubbard, J. R., Martin, B. R., and Kalimi, M. Y. (1993) Roles of sulfhydryl and disulfide groups in the binding of CP-55,940 to rat brain cannabinoid receptor, Mol. Cell. Biochem. 121, 119-126.
    • (1993) Mol. Cell. Biochem. , vol.121 , pp. 119-126
    • Lu, R.1    Hubbard, J.R.2    Martin, B.R.3    Kalimi, M.Y.4
  • 18
    • 0029965292 scopus 로고    scopus 로고
    • Structural features of the central cannabinoid CB1 receptor involved in the binding of the specific CB1 antagonist SR 141716A
    • Shire, D., Calandra, B., Delpech, M., Dumont, X., Kaghad, M., Le Fur, G., Caput, D., and Ferrara, P. (1996) Structural features of the central cannabinoid CB1 receptor involved in the binding of the specific CB1 antagonist SR 141716A, J. Biol. Chem. 271, 6941-6946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6941-6946
    • Shire, D.1    Calandra, B.2    Delpech, M.3    Dumont, X.4    Kaghad, M.5    Le Fur, G.6    Caput, D.7    Ferrara, P.8
  • 19
    • 0037142337 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationships of amide and hydrazide analogues of the cannabinoid CB(1) receptor antagonist N-(piperidinyl)-5-(4- chlorophenyl)-1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide (SR141716)
    • Francisco, M. E., Seltzman, H. H., Gilliam, A. F., Mitchell, R. A., Rider, S. L., Pertwee, R. G., Stevenson, L. A., and Thomas, B. F. (2002) Synthesis and structure-activity relationships of amide and hydrazide analogues of the cannabinoid CB(1) receptor antagonist N-(piperidinyl)-5-(4-chlorophenyl)- 1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide (SR141716), J. Med. Chem. 45, 2708-2719.
    • (2002) J. Med. Chem. , vol.45 , pp. 2708-2719
    • Francisco, M.E.1    Seltzman, H.H.2    Gilliam, A.F.3    Mitchell, R.A.4    Rider, S.L.5    Pertwee, R.G.6    Stevenson, L.A.7    Thomas, B.F.8
  • 20
    • 77957055780 scopus 로고
    • Integrated methods for modeling G-protein coupled receptors
    • Ballesteros, J. A., and Weinstein, H. (1995) Integrated Methods for Modeling G-Protein Coupled Receptors, Methods Neurosci. 25, 366-428.
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 21
    • 0036945737 scopus 로고    scopus 로고
    • Design, expression, and characterization of a synthetic human cannabinoid receptor and cannabinoid receptor/G-protein fusion protein
    • Farrens, D. L., Dunham, T. D., Fay, J. F., Dews, I. C., Caldwell, J., and Nauert, B. (2002) Design, expression, and characterization of a synthetic human cannabinoid receptor and cannabinoid receptor/G-protein fusion protein, J. Pept. Res. 60, 336-347.
    • (2002) J. Pept. Res. , vol.60 , pp. 336-347
    • Farrens, D.L.1    Dunham, T.D.2    Fay, J.F.3    Dews, I.C.4    Caldwell, J.5    Nauert, B.6
  • 23
    • 0038037706 scopus 로고    scopus 로고
    • Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2
    • Janz, J. M., Fay, J. F., and Farrens, D. L. (2003) Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2, J. Biol. Chem. 278, 16982-16991.
    • (2003) J. Biol. Chem. , vol.278 , pp. 16982-16991
    • Janz, J.M.1    Fay, J.F.2    Farrens, D.L.3
  • 24
    • 0029012098 scopus 로고
    • Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis
    • Swillens, S. (1995) Interpretation of binding curves obtained with high receptor concentrations: Practical aid for computer analysis, Mol. Pharmacol. 47, 1197-1203.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 1197-1203
    • Swillens, S.1
  • 25
    • 0024332759 scopus 로고
    • Calculating receptor number from binding experiments using same compound as radioligand and competitor
    • DeBlasi, A., O'Reilly, K., and Motulsky, H. J. (1989) Calculating receptor number from binding experiments using same compound as radioligand and competitor, Trends Pharmacol. Sci. 10, 227-229.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 227-229
    • DeBlasi, A.1    O'Reilly, K.2    Motulsky, H.J.3
  • 26
    • 0034792329 scopus 로고    scopus 로고
    • Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors
    • Javitch, J. A., Shi, L., and Liapakis, G. (2002) Use of the substituted cysteine accessibility method to study the structure and function of G protein-coupled receptors, Methods Enzymol. 343, 137-156.
    • (2002) Methods Enzymol. , vol.343 , pp. 137-156
    • Javitch, J.A.1    Shi, L.2    Liapakis, G.3
  • 28
    • 0036954833 scopus 로고    scopus 로고
    • Activation of the cannabinoid CB1 receptor may involve a W6 48/F3 36 rotamer toggle switch
    • Singh, R., Hurst, D. P., Barnett-Norris, J., Lynch, D. L., Reggio, P. H., and Guarnieri, F. (2002) Activation of the cannabinoid CB1 receptor may involve a W6 48/F3 36 rotamer toggle switch, J. Pept. Res. 60, 357-370.
    • (2002) J. Pept. Res. , vol.60 , pp. 357-370
    • Singh, R.1    Hurst, D.P.2    Barnett-Norris, J.3    Lynch, D.L.4    Reggio, P.H.5    Guarnieri, F.6
  • 31
    • 0025885547 scopus 로고
    • Depalmitylation with hydroxylamine alters the functional properties of rhodopsin
    • Morrison, D. F., O'Brien, P. J., and Pepperberg, D. R. (1991) Depalmitylation with hydroxylamine alters the functional properties of rhodopsin. J. Biol. Chem. 266, 20118-20123.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20118-20123
    • Morrison, D.F.1    O'Brien, P.J.2    Pepperberg, D.R.3
  • 32
    • 0034695476 scopus 로고    scopus 로고
    • The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction
    • Marin, E. P., Krishna, A. G., Zvyaga, T. A., Isele, J., Siebert, F., and Sakmar, T. P. (2000) The amino terminus of the fourth cytoplasmic loop of rhodopsin modulates rhodopsin-transducin interaction, J. Biol. Chem. 275, 1930-1936.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1930-1936
    • Marin, E.P.1    Krishna, A.G.2    Zvyaga, T.A.3    Isele, J.4    Siebert, F.5    Sakmar, T.P.6
  • 33
    • 0031594615 scopus 로고    scopus 로고
    • Characterization of CB1 cannabinoid receptors using receptor peptide fragments and site-directed antibodies
    • Hewlett, A. C., Song, C., Berglund, B. A., Wilken, G. H., and Pigg, J. J. (1998) Characterization of CB1 cannabinoid receptors using receptor peptide fragments and site-directed antibodies, Mol. Pharmacol. 53, 504-510.
    • (1998) Mol. Pharmacol. , vol.53 , pp. 504-510
    • Hewlett, A.C.1    Song, C.2    Berglund, B.A.3    Wilken, G.H.4    Pigg, J.J.5
  • 34
    • 0033574084 scopus 로고    scopus 로고
    • Regulation of Gi by the CB1 cannabinoid receptor C-terminal juxtamembrane region: Structural requirements determined by peptide analysis
    • Mukhopadhyay, S., Cowsik, S. M., Lynn, A. M., Welsh, W. J., and Howlett, A. C. (1999) Regulation of Gi by the CB1 cannabinoid receptor C-terminal juxtamembrane region: Structural requirements determined by peptide analysis, Biochemistry 38. 3447-3455.
    • (1999) Biochemistry , vol.38 , pp. 3447-3455
    • Mukhopadhyay, S.1    Cowsik, S.M.2    Lynn, A.M.3    Welsh, W.J.4    Howlett, A.C.5
  • 35
    • 0035919754 scopus 로고    scopus 로고
    • Functional roles of the tyrosine within the NP(X)(n)Y motif and the cysteines in the C-terminal juxtamembrane region of the CB2 cannabinoid receptor
    • Feng, W., and Song, Z. H. (2001) Functional roles of the tyrosine within the NP(X)(n)Y motif and the cysteines in the C-terminal juxtamembrane region of the CB2 cannabinoid receptor, FEBS Lett. 501, 166-170.
    • (2001) FEBS Lett. , vol.501 , pp. 166-170
    • Feng, W.1    Song, Z.H.2
  • 36
    • 0023055733 scopus 로고
    • Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate
    • Roberts, D. D., Lewis, S. D., Ballou, D. P., Olson, S. T., and Shafer, J. A. (1986) Reactivity of small thiolate anions and cysteine-25 in papain toward methyl methanethiosulfonate, Biochemistry 25, 5595-5601.
    • (1986) Biochemistry , vol.25 , pp. 5595-5601
    • Roberts, D.D.1    Lewis, S.D.2    Ballou, D.P.3    Olson, S.T.4    Shafer, J.A.5
  • 41
    • 0029757635 scopus 로고    scopus 로고
    • Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice
    • Fu, D., Ballesteros, J. A., Weinstein, H., Chen, J., and Javitch, J. A. (1996) Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice, Biochemistry 35, 11278-11285.
    • (1996) Biochemistry , vol.35 , pp. 11278-11285
    • Fu, D.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.4    Javitch, J.A.5
  • 42
    • 0027104740 scopus 로고
    • Identification of a single amino acid residue responsible for the binding of a class of β-adrenergic receptor antagonists to 5-hydroxytryptamine 1A receptors
    • Guan, X. M., Peroutka, S. J., and Kobilka, B. K. (1992) Identification of a single amino acid residue responsible for the binding of a class of β-adrenergic receptor antagonists to 5-hydroxytryptamine 1A receptors, Mol. Pharmacol. 41, 695-698.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 695-698
    • Guan, X.M.1    Peroutka, S.J.2    Kobilka, B.K.3
  • 43
    • 0026362961 scopus 로고
    • A single point mutation in the seventh hydrophobic domain of the α2-adrenergic receptor changes antagonist binding specificity to that of a β receptor
    • Suryanarayana, S., Daunt, D. A., Von Zastrow, M., and Kobilka, B. K. (1991) A single point mutation in the seventh hydrophobic domain of the α2-adrenergic receptor changes antagonist binding specificity to that of a β receptor, Trans. Assoc. Am. Physicians 104, 62-68.
    • (1991) Trans. Assoc. Am. Physicians , vol.104 , pp. 62-68
    • Suryanarayana, S.1    Daunt, D.A.2    Von Zastrow, M.3    Kobilka, B.K.4
  • 44
    • 0025744363 scopus 로고
    • A point mutation in the seventh hydrophobic domain of the α2 adrenergic receptor increases its affinity for a family of β receptor antagonists
    • Suryanarayana, S., Daunt, D. A., Von Zastrow, M., and Kobilka, B. K. (1991) A point mutation in the seventh hydrophobic domain of the α2 adrenergic receptor increases its affinity for a family of β receptor antagonists. J. Biol. Chem. 266, 15488-15492.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15488-15492
    • Suryanarayana, S.1    Daunt, D.A.2    Von Zastrow, M.3    Kobilka, B.K.4
  • 45
    • 0027296745 scopus 로고
    • Amino acid substitutions at position 312 in the seventh hydrophobic segment of the β2-adrenergic receptor modify ligand-binding specificity
    • Suryanarayana, S., and Kobilka, B. K. (1993) Amino acid substitutions at position 312 in the seventh hydrophobic segment of the β2-adrenergic receptor modify ligand-binding specificity, Mol. Pharmacol. 44, 111-114.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 111-114
    • Suryanarayana, S.1    Kobilka, B.K.2
  • 46
    • 0030742276 scopus 로고    scopus 로고
    • Identification of conserved aromatic residues essential for agonist binding and second messenger production at 5-hydroxytryptamine 2A receptors
    • Roth, B. L., Shoham, M., Choudhary, M. S., and Khan, N. (1997) Identification of conserved aromatic residues essential for agonist binding and second messenger production at 5-hydroxytryptamine 2A receptors, Mol. Pharmacol. 52, 259-266.
    • (1997) Mol. Pharmacol. , vol.52 , pp. 259-266
    • Roth, B.L.1    Shoham, M.2    Choudhary, M.S.3    Khan, N.4
  • 47
    • 0035037874 scopus 로고    scopus 로고
    • Determination of amino acid residues that are accessible from the ligand binding crevice in the seventh transmembrane-spanning region of the human A(1) adenosine receptor
    • Dawson, E. S., and Wells, J. N. (2001) Determination of amino acid residues that are accessible from the ligand binding crevice in the seventh transmembrane-spanning region of the human A(1) adenosine receptor, Mol. Pharmacol. 59, 1187-1195.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 1187-1195
    • Dawson, E.S.1    Wells, J.N.2
  • 48
    • 0032723795 scopus 로고    scopus 로고
    • Dopamine D4/D2 receptor selectivity is determined by a divergent aromatic microdomain contained within the second, third, and seventh membrane-spanning segments
    • Simpson, M. M., Ballesteros, J. A., Chiappa, V., Chen, J., Suehiro, M., Hartman, D. S., Godel, T., Snyder, L. A., Sakmar, T. P., and Javitch, J. A. (1999) Dopamine D4/D2 receptor selectivity is determined by a divergent aromatic microdomain contained within the second, third, and seventh membrane-spanning segments, Mol. Pharmacol. 56, 1116-1126.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1116-1126
    • Simpson, M.M.1    Ballesteros, J.A.2    Chiappa, V.3    Chen, J.4    Suehiro, M.5    Hartman, D.S.6    Godel, T.7    Snyder, L.A.8    Sakmar, T.P.9    Javitch, J.A.10
  • 49
    • 0034649373 scopus 로고    scopus 로고
    • The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the μ, δ, and κ opoid receptors
    • Xu, W., Chen, C., Huang, P., Li, J., de Kiel, J. K., Javitch, J. A., and Liu-Chen, L. Y. (2000) The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the μ, δ, and κ opoid receptors, Biochemistry 39, 13904-13915.
    • (2000) Biochemistry , vol.39 , pp. 13904-13915
    • Xu, W.1    Chen, C.2    Huang, P.3    Li, J.4    De Kiel, J.K.5    Javitch, J.A.6    Liu-Chen, L.Y.7
  • 50
    • 0029993990 scopus 로고    scopus 로고
    • Activating mutations of rhodopsin and other G protein-coupled receptors
    • Rao, V. R., and Oprian, D. D. (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
  • 52
    • 0027248024 scopus 로고
    • Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness
    • Dryja, T. P., Berson, E. L., Rao, V. R., and Oprian, D. D. (1993) Heterozygous missense mutation in the rhodopsin gene as a cause of congenital stationary night blindness, Nat. Genet. 4, 280-283.
    • (1993) Nat. Genet. , vol.4 , pp. 280-283
    • Dryja, T.P.1    Berson, E.L.2    Rao, V.R.3    Oprian, D.D.4
  • 55
    • 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., Yang, K., Farrens, D. L., Farahbakhsh, Z. T., Khorana, H. G., and Hubbell, W. L. (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
  • 56
    • 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
  • 57
    • 0029778268 scopus 로고    scopus 로고
    • Rhodopsin activation blocked by metalion-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 metalion-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
  • 58
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the β2 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 β2 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
  • 59
    • 0033555936 scopus 로고    scopus 로고
    • Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy
    • Dunham, T. D., and Farrens, D. L. (1999) Conformational changes in rhodopsin. Movement of helix f detected by site-specific chemical labeling and fluorescence spectroscopy, J. Biol. Chem. 274, 1683-1690.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1683-1690
    • Dunham, T.D.1    Farrens, D.L.2
  • 60
    • 3142773613 scopus 로고    scopus 로고
    • Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus
    • Janz, J. M., and Farrens, D. L. (2004) Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus, J. Biol. Chem. 279, 29767-29773.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29767-29773
    • Janz, J.M.1    Farrens, D.L.2
  • 62
    • 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
  • 63
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W. L., Altenbach, C., Hubbell, C. M., and Khorana, H. G. (2003) Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking, Adv. Protein Chem. 63, 243-290.
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 64
    • 0037414446 scopus 로고    scopus 로고
    • Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study
    • Alexiev, U., Rimke, I., and Pohlmann, T. (2003) Elucidation of the nature of the conformational changes of the EF-interhelical loop in bacteriorhodopsin and of the helix VIII on the cytoplasmic surface of bovine rhodopsin: A time-resolved fluorescence depolarization study, J. Mol. Biol. 328, 705-719.
    • (2003) J. Mol. Biol. , vol.328 , pp. 705-719
    • Alexiev, U.1    Rimke, I.2    Pohlmann, T.3
  • 65
    • 0034642188 scopus 로고    scopus 로고
    • Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface
    • Imamoto, Y., Kataoka, M., Tokunaga, F., and Palczewski, K. (2000) Light-induced conformational changes of rhodopsin probed by fluorescent alexa594 immobilized on the cytoplasmic surface, Biochemistry 39, 15225-15233.
    • (2000) Biochemistry , vol.39 , pp. 15225-15233
    • Imamoto, Y.1    Kataoka, M.2    Tokunaga, F.3    Palczewski, K.4
  • 66
    • 0032573218 scopus 로고    scopus 로고
    • Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin
    • Abdulaev, N. G., and Ridge, K. D. (1998) Light-induced exposure of the cytoplasmic end of transmembrane helix seven in rhodopsin, Proc. Natl. Acad. Sci. U.S.A. 95, 12854-12859.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 12854-12859
    • Abdulaev, N.G.1    Ridge, K.D.2
  • 68
    • 0037192858 scopus 로고    scopus 로고
    • Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6
    • Shapiro, D. A., Kristiansen, K., Weiner, D. M., Kroeze, W. K., and Roth, B. L. (2002) Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6, J. Biol. Chem. 277, 11441-11449.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11441-11449
    • Shapiro, D.A.1    Kristiansen, K.2    Weiner, D.M.3    Kroeze, W.K.4    Roth, B.L.5
  • 69
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros, J. A., Jensen, A. D., Liapakis, G., Rasmussen, S. G., Shi, L., Gether, U., and Javitch, J. A. (2001) Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6, J. Biol. Chem. 276, 29171-29177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 70
    • 0035793604 scopus 로고    scopus 로고
    • An activation switch in the ligand binding pocket of the C5a receptor
    • Gerber, B. O., Meng, E. C., Dotsch, V., Baranski, T. J., and Bourne, H. R. (2001) An activation switch in the ligand binding pocket of the C5a receptor, J. Biol. Chem. 276, 3394-3400.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3394-3400
    • Gerber, B.O.1    Meng, E.C.2    Dotsch, V.3    Baranski, T.J.4    Bourne, H.R.5
  • 71
    • 0242488918 scopus 로고    scopus 로고
    • Evolutionary analysis of rhodopsin and cone pigments: Connecting the three-dimensional structure with spectral tuning and signal transfer
    • Teller, D. C., Stenkamp, R. E., and Palczewski, K. (2003) Evolutionary analysis of rhodopsin and cone pigments: Connecting the three-dimensional structure with spectral tuning and signal transfer, FEBS Lett. 555, 151-159.
    • (2003) FEBS Lett. , vol.555 , pp. 151-159
    • Teller, D.C.1    Stenkamp, R.E.2    Palczewski, K.3
  • 73
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Ballesteros, J. A., Shi, L., and Javitch, J. A. (2001) Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors, Mol. Pharmacol. 60, 1-19.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 74
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers, I., Ballesteros, J. A., and Weinstein, H. (2002) Three-dimensional representations of G protein-coupled receptor structures and mechanisms, Methods Enzymol. 343, 329-371.
    • (2002) Methods Enzymol. , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 75
    • 0345791508 scopus 로고    scopus 로고
    • Sequential binding of agonists to the β2 adrenoceptor. Kinetic evidence for intermediate conformational states
    • Swaminath, G., Xiang, Y., Lee, T. W., Steenhuis, J., Parnot, C., and Kobilka, B. K. (2004) Sequential binding of agonists to the β2 adrenoceptor. Kinetic evidence for intermediate conformational states, J. Biol. Chem. 279, 686-691.
    • (2004) J. Biol. Chem. , vol.279 , pp. 686-691
    • Swaminath, G.1    Xiang, Y.2    Lee, T.W.3    Steenhuis, J.4    Parnot, C.5    Kobilka, B.K.6
  • 76
    • 0036950338 scopus 로고    scopus 로고
    • Ligand based structural studies of the CB1 cannabinoid receptor
    • Picone, R. P., Fournier, D. J., Makriyannis, A. (2002) Ligand based structural studies of the CB1 cannabinoid receptor. J. Pept. Res. 60, 348-356.
    • (2002) J. Pept. Res. , vol.60 , pp. 348-356
    • Picone, R.P.1    Fournier, D.J.2    Makriyannis, A.3
  • 77
    • 6344248911 scopus 로고    scopus 로고
    • Current and investigational antiobesity agents and obesity therapeutic treatment targets
    • Bays, H. E. (2004) Current and investigational antiobesity agents and obesity therapeutic treatment targets, Obes. Res. 12, 1197-1211.
    • (2004) Obes. Res. , vol.12 , pp. 1197-1211
    • Bays, H.E.1
  • 78
    • 0032321487 scopus 로고    scopus 로고
    • Substituted-cysteine accessibility method
    • Karlin, A., and Akabas, M. H. (1998) Substituted-cysteine accessibility method, Methods Enzymol. 293, 123 -145.
    • (1998) Methods Enzymol. , vol.293 , pp. 123-145
    • Karlin, A.1    Akabas, M.H.2
  • 79
    • 0026485739 scopus 로고
    • Acetylcholine receptor channel structure probed in cysteine-substitution mutants
    • Akabas, M. H., Stauffer, D. A., Xu, M., and Karlin, A. (1992) Acetylcholine receptor channel structure probed in cysteine-substitution mutants, Science 258, 307-310.
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 80
    • 0037187367 scopus 로고    scopus 로고
    • Molecular interaction of the antagonist N-(piperidin-1-y1)-5-(4- chlorophenyl)-1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide with the CB1 cannabinoid receptor
    • Shim, J. Y., Welsh, W. J., Cartier, E., Edwards, J. L., and Howlett, A. C. (2002) Molecular interaction of the antagonist N-(piperidin-1-y1)-5-(4- chlorophenyl)-1-(2,4-dichlorophenyl)-4-methyl-1H-pyrazole-3-carboxamide with the CB1 cannabinoid receptor, J. Med. Chem. 45, 1447-1459.
    • (2002) J. Med. Chem. , vol.45 , pp. 1447-1459
    • Shim, J.Y.1    Welsh, W.J.2    Cartier, E.3    Edwards, J.L.4    Howlett, A.C.5
  • 81
    • 9144224914 scopus 로고    scopus 로고
    • Structural mimicry in class a protein-coupled receptor rotamer toggle switches: The importance of the F3.36(201)/W6.48(357) interaction in cannabinoid CB1 receptor activation
    • McAllister, S. D., Hurst, D. P., Barnett-Norris, J., Lynch, D., Reggio, P. H., and Abood, M. E. (2004) Structural mimicry in class A protein-coupled receptor rotamer toggle switches: The importance of the F3.36(201)/W6.48(357) interaction in cannabinoid CB1 receptor activation, J. Biol. Chem. 279, 48024-48037.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48024-48037
    • McAllister, S.D.1    Hurst, D.P.2    Barnett-Norris, J.3    Lynch, D.4    Reggio, P.H.5    Abood, M.E.6
  • 82
    • 0032771955 scopus 로고    scopus 로고
    • Internalization and recycling of the CB1 cannabinoid receptor
    • Hsieh, C., Brown, S., Derleth, C., Mackie, K. (1999) Internalization and recycling of the CB1 cannabinoid receptor. J. Neurochem. 73, 493-501.
    • (1999) J. Neurochem. , vol.73 , pp. 493-501
    • Hsieh, C.1    Brown, S.2    Derleth, C.3    Mackie, K.4
  • 83
    • 3042780243 scopus 로고    scopus 로고
    • Identification of a potent and highly efficacious, yet slowly desensitizing CB1 cannabinoid receptor agonist
    • Luk, T., Jin, W., Zvonok, A., Lu, D., Lin, X. Z., Chavkin, C., Makriyannis, A., Mackie, K. (2004) Identification of a potent and highly efficacious, yet slowly desensitizing CB1 cannabinoid receptor agonist. Br. J. Pharmacol. 142, 495-500.
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 495-500
    • Luk, T.1    Jin, W.2    Zvonok, A.3    Lu, D.4    Lin, X.Z.5    Chavkin, C.6    Makriyannis, A.7    Mackie, K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.