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Volumn 138, Issue 7, 1997, Pages 2800-2806

An intramolecular disulfide bond between conserved extracellular cysteines in the gonadotropin-releasing hormone receptor is essential for binding and activation

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; CYSTEINE; EPITOPE; GONADORELIN; GONADORELIN RECEPTOR;

EID: 0030917971     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.138.7.5233     Document Type: Article
Times cited : (97)

References (33)
  • 2
    • 0026794339 scopus 로고
    • Molecular cloning and expression of cDNA encoding the murine gonadotropin releasing hormone receptor
    • Reinhart J, Mertz LM, Catt K 1992 Molecular cloning and expression of cDNA encoding the murine gonadotropin releasing hormone receptor. J Biol Chem 267:21281-21284
    • (1992) J Biol Chem , vol.267 , pp. 21281-21284
    • Reinhart, J.1    Mertz, L.M.2    Catt, K.3
  • 3
    • 0026446941 scopus 로고
    • Molecular cloning and characterisation of the rat pituitary gonadotrophin-releasing hormone (GnRH) receptor
    • Eidne KA, Sellar RE, Couper G, Anderson L, Taylor PL 1992 Molecular cloning and characterisation of the rat pituitary gonadotrophin-releasing hormone (GnRH) receptor. Mol Cell Endocrinol 90:R5-R9
    • (1992) Mol Cell Endocrinol , vol.90
    • Eidne, K.A.1    Sellar, R.E.2    Couper, G.3    Anderson, L.4    Taylor, P.L.5
  • 4
    • 0027053396 scopus 로고
    • Isolation and characterization of the cDNAs encoding the rat pituitary gonadotropin-releasing hormone receptor
    • Kaiser UB, Zhao D, Cardona RG, Chin WW 1992 Isolation and characterization of the cDNAs encoding the rat pituitary gonadotropin-releasing hormone receptor. Biochem Biophys Res Commun 189:1645-1652
    • (1992) Biochem Biophys Res Commun , vol.189 , pp. 1645-1652
    • Kaiser, U.B.1    Zhao, D.2    Cardona, R.G.3    Chin, W.W.4
  • 8
    • 0027244644 scopus 로고
    • Cloning and sequencing of the sheep pituitary gonadotropin-releasing hormone receptor and changes in expression of its mRNA during the estrous cycle
    • Brooks J, Taylor PL, Saunders P, Eidne KA, Struthers WJ, McNeilly AS 1993 Cloning and sequencing of the sheep pituitary gonadotropin-releasing hormone receptor and changes in expression of its mRNA during the estrous cycle. Mol Cell Endocrinol 94:R1-R6
    • (1993) Mol Cell Endocrinol , vol.94
    • Brooks, J.1    Taylor, P.L.2    Saunders, P.3    Eidne, K.A.4    Struthers, W.J.5    McNeilly, A.S.6
  • 9
    • 0027378202 scopus 로고
    • Comparative sequence analysis and functional characterization of the cloned sheep gonadotropin-releasing hormone receptor reveals differences in primary structure and ligand specificity among mammalian receptors
    • Illing N, Jacobs GFM, Becker II, Flanagan CA, Davidson JS, Eales A, Sealfon SC 1993 Comparative sequence analysis and functional characterization of the cloned sheep gonadotropin-releasing hormone receptor reveals differences in primary structure and ligand specificity among mammalian receptors. Biochem Biophys Res Commun 196:745-751
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 745-751
    • Illing, N.1    Jacobs, G.F.M.2    Becker, I.I.3    Flanagan, C.A.4    Davidson, J.S.5    Eales, A.6    Sealfon, S.C.7
  • 10
    • 0027674399 scopus 로고
    • Molecular cloning, sequencing and characterizing the bovine receptor for the gonadotropin-releasing hormone (GnRH)
    • Kakar SS, Rahe CH, Neill JD 1993 Molecular cloning, sequencing and characterizing the bovine receptor for the gonadotropin-releasing hormone (GnRH). Dom Anim Endocrinol 10:335-342
    • (1993) Dom Anim Endocrinol , vol.10 , pp. 335-342
    • Kakar, S.S.1    Rahe, C.H.2    Neill, J.D.3
  • 11
    • 0028472357 scopus 로고
    • Nucleotide sequence of luteinizing hormone-releasing hormone (LHRH) receptor cDNA in pig pituitary
    • Weesner GD, Matteri RL 1994 Nucleotide sequence of luteinizing hormone-releasing hormone (LHRH) receptor cDNA in pig pituitary. J Anim Sci 72:1911
    • (1994) J Anim Sci , vol.72 , pp. 1911
    • Weesner, G.D.1    Matteri, R.L.2
  • 13
    • 0028227013 scopus 로고
    • Structure and function of receptors coupled to G-proteins
    • Baldwin JM 1994 Structure and function of receptors coupled to G-proteins. Curr Opin Cell Biol 6:180-190
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 180-190
    • Baldwin, J.M.1
  • 14
    • 0025249790 scopus 로고
    • Role of extracellular disulfide-bonded cysteines in the ligand binding function of the β2 adrenergic receptor
    • Dohlman HG, Caron MG, Deblasi A, Freille T, Lefkowitz RJ 1990 Role of extracellular disulfide-bonded cysteines in the ligand binding function of the β2 adrenergic receptor. Biochemistry 29:2335-2342
    • (1990) Biochemistry , vol.29 , pp. 2335-2342
    • Dohlman, H.G.1    Caron, M.G.2    Deblasi, A.3    Freille, T.4    Lefkowitz, R.J.5
  • 15
    • 0028318173 scopus 로고
    • The high affinity state of the β2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines
    • Noda K, Saad Y, Grahem RM, Karnik SS 1994 The high affinity state of the β2-adrenergic receptor requires unique interaction between conserved and non-conserved extracellular loop cysteines. J Biol Chem 269:6743-6752
    • (1994) J Biol Chem , vol.269 , pp. 6743-6752
    • Noda, K.1    Saad, Y.2    Grahem, R.M.3    Karnik, S.S.4
  • 16
    • 0024110575 scopus 로고
    • Cysteine residues 110 and 187 are essential for the formation of the correct structure of bovine rhodopsin
    • Karnik SS, Sakmar TP, Chen H-B, Khorana GH 1988 Cysteine residues 110 and 187 are essential for the formation of the correct structure of bovine rhodopsin. Proc Natl Acad Sci USA 85:8859-8459
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8859-18459
    • Karnik, S.S.1    Sakmar, T.P.2    Chen, H.-B.3    Khorana, G.H.4
  • 17
    • 0028351937 scopus 로고
    • Structure and function in rhodopsin: Replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state
    • Davidson FF, Loewen PC, Khorana HG 1994 Structure and function in rhodopsin: Replacement by alanine of cysteine residues 110 and 187, components of a conserved disulfide bond in rhodopsin, affects the light-activated metarhodopsin II state. Proc Natl Acad Sci USA 91:4029-4033
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4029-4033
    • Davidson, F.F.1    Loewen, P.C.2    Khorana, H.G.3
  • 18
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TA 1987 Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82:488-492
    • (1987) Proc Natl Acad Sci USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 19
    • 0019309669 scopus 로고
    • Leydig cell receptors for luteinising hormone releasing hormone and its agonists and their modulation by administration of depriving of the releasing hormone
    • Sharpe RM, Fraser HM 1980 Leydig cell receptors for luteinising hormone releasing hormone and its agonists and their modulation by administration of depriving of the releasing hormone. Biochem Biophys Res Commun 95:256-262
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 256-262
    • Sharpe, R.M.1    Fraser, H.M.2
  • 20
    • 0026639831 scopus 로고
    • Site-directed mutagenesis of the rat m1 muscarinic acecylcholine receptor
    • Savarese TM, Wang C-D, Fraser C 1992 Site-directed mutagenesis of the rat m1 muscarinic acecylcholine receptor. J Biol Chem 267:11439-11448
    • (1992) J Biol Chem , vol.267 , pp. 11439-11448
    • Savarese, T.M.1    Wang, C.-D.2    Fraser, C.3
  • 21
    • 0026666733 scopus 로고
    • Identification of amino acid residues of the rat angiotensin II receptor for ligand binding by site directed mutagenesis
    • Yamano Y, Ohyama K, Chaki S, Guo D-F, Inagami T 1992 Identification of amino acid residues of the rat angiotensin II receptor for ligand binding by site directed mutagenesis. Biochem Biophys Res Commun 187:1426-1431
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 1426-1431
    • Yamano, Y.1    Ohyama, K.2    Chaki, S.3    Guo, D.-F.4    Inagami, T.5
  • 22
    • 0029894178 scopus 로고    scopus 로고
    • A disulfide bonding interaction role for cysteines in the extracellular domain of the thyrotropin-releasing hormone receptor
    • Cook JVF, McGregor A, Lee T-W, Milligan G, Eidne KA 1996 A disulfide bonding interaction role for cysteines in the extracellular domain of the thyrotropin-releasing hormone receptor. Endocrinology 137:2851-2858
    • (1996) Endocrinology , vol.137 , pp. 2851-2858
    • Cook, J.V.F.1    McGregor, A.2    Lee, T.-W.3    Milligan, G.4    Eidne, K.A.5
  • 23
    • 0028808101 scopus 로고    scopus 로고
    • A disulfide bond between conserved extracellular cysteines in the thyrotropin-releasing hormone receptor is critical for binding
    • Perlman JH, Wang W, Nussenzveig DR, Gershengorn MC 1996 A disulfide bond between conserved extracellular cysteines in the thyrotropin-releasing hormone receptor is critical for binding. J Biol Chem 270:24682-24685
    • (1996) J Biol Chem , vol.270 , pp. 24682-24685
    • Perlman, J.H.1    Wang, W.2    Nussenzveig, D.R.3    Gershengorn, M.C.4
  • 24
    • 0022295633 scopus 로고
    • Mapping of the gonadotropin-releasing hormone receptor binding site
    • Keinan D, Hazum E 1985 Mapping of the gonadotropin-releasing hormone receptor binding site. Biochemistry 24:7728-7732
    • (1985) Biochemistry , vol.24 , pp. 7728-7732
    • Keinan, D.1    Hazum, E.2
  • 25
    • 0027787795 scopus 로고
    • Effects of Asn87 and Asp318 mutations on ligand binding and signal transduction in the rat GnRH receptor
    • Cook JV, Faccenda E, Anderson L, Couper G, Eidne KA, Taylor PL 1993 Effects of Asn87 and Asp318 mutations on ligand binding and signal transduction in the rat GnRH receptor. J Endocrinol 139:R1-R4
    • (1993) J Endocrinol , vol.139
    • Cook, J.V.1    Faccenda, E.2    Anderson, L.3    Couper, G.4    Eidne, K.A.5    Taylor, P.L.6
  • 26
    • 0023100261 scopus 로고
    • Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
    • Yarden Y, Schlessinger J 1987 Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor. Biochemistry 26:1443-1451
    • (1987) Biochemistry , vol.26 , pp. 1443-1451
    • Yarden, Y.1    Schlessinger, J.2
  • 27
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich A, Schlessinger J 1990 Signal transduction by receptors with tyrosine kinase activity. Cell 61:203-212
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 28
    • 0029922265 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in the Class 1 disulphide bonds of the human insulin receptor: Properties of insulin receptor monomers
    • Lu K, Guidotti G 1996 Identification of the cysteine residues involved in the Class 1 disulphide bonds of the human insulin receptor: Properties of insulin receptor monomers. Mol Biol Cell 7:679-691
    • (1996) Mol Biol Cell , vol.7 , pp. 679-691
    • Lu, K.1    Guidotti, G.2
  • 29
    • 0022665939 scopus 로고
    • Gonadotropin-releasing hormone analog design. Structure-function studies towards the development of agonists and antagonists: Rationale and perspectives
    • Karten MJ, Rivier JE 1986 Gonadotropin-releasing hormone analog design. Structure-function studies towards the development of agonists and antagonists: rationale and perspectives. Endocr Rev 7:44-66
    • (1986) Endocr Rev , vol.7 , pp. 44-66
    • Karten, M.J.1    Rivier, J.E.2
  • 30
    • 0023864155 scopus 로고
    • Photoaffinity labeling of pituitary GnRH receptors: Significance and position of photolabel on the ligand
    • Nikolics K, Szonyi E, Ramachandran J 1988 Photoaffinity labeling of pituitary GnRH receptors: significance and position of photolabel on the ligand. Biochemistry 27:1425-1432
    • (1988) Biochemistry , vol.27 , pp. 1425-1432
    • Nikolics, K.1    Szonyi, E.2    Ramachandran, J.3
  • 32
    • 0027498242 scopus 로고
    • Characterisation of the gonadotropin-releasing hormone receptor in α-T3-1 pituitary gonadotroph cells
    • Anderson L, Milligan G, Eidne KA 1993 Characterisation of the gonadotropin-releasing hormone receptor in α-T3-1 pituitary gonadotroph cells. J Endocrinol 136:51-58
    • (1993) J Endocrinol , vol.136 , pp. 51-58
    • Anderson, L.1    Milligan, G.2    Eidne, K.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.