메뉴 건너뛰기




Volumn 579, Issue 1, 2005, Pages 285-291

MTSEA prevents ligand binding to the human melanocortin-4 receptor by modification of cysteine 130 in transmembrane helix 3

Author keywords

MSH; G protein coupled receptor; Melanocortin 4 receptor; MTSEA

Indexed keywords

ALANINE; AMMONIUM DERIVATIVE; CYSTEINE DERIVATIVE; INTERMEDIN; IODINE 125; MELANOCORTIN 4 RECEPTOR; N ACETYL ALPHA INTERMEDIN[4-10]CYCLO[4 NORLEUCINE 5 ASPARTIC ACID 7 [3 (2 NAPHTHYL)ALANINE] 10 LYSINAMIDE]; THIOL REAGENT;

EID: 11144296970     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.11.087     Document Type: Article
Times cited : (2)

References (27)
  • 1
    • 0026800892 scopus 로고
    • The cloning of a family of genes that encode the melanocortin receptors
    • K.G. Mountjoy, L.S. Robbins, M.T. Mortrud, and R.D. Cone The cloning of a family of genes that encode the melanocortin receptors Science 257 1992 1248 1251
    • (1992) Science , vol.257 , pp. 1248-1251
    • Mountjoy, K.G.1    Robbins, L.S.2    Mortrud, M.T.3    Cone, R.D.4
  • 3
    • 0031442053 scopus 로고    scopus 로고
    • Exocrine gland dysfunction in MC5-R-deficient mice: Evidence for coordinated regulation of exocrine gland function by melanocortin peptides
    • W.B. Chen, M.A. Kelly, X. OpitzAraya, R.E. Thomas, M.J. Low, and R.D. Cone Exocrine gland dysfunction in MC5-R-deficient mice: Evidence for coordinated regulation of exocrine gland function by melanocortin peptides Cell 91 1997 789 798
    • (1997) Cell , vol.91 , pp. 789-798
    • Chen, W.B.1    Kelly, M.A.2    Opitzaraya, X.3    Thomas, R.E.4    Low, M.J.5    Cone, R.D.6
  • 4
    • 0028134706 scopus 로고
    • Localization of the Melanocortin-4 Receptor (Mc4-R) in Neuroendocrine and Autonomic Control-Circuits in the Brain
    • K.G. Mountjoy, M.T. Mortrud, M.J. Low, R.B. Simerly, and R.D. Cone Localization of the Melanocortin-4 Receptor (Mc4-R) in Neuroendocrine and Autonomic Control-Circuits in the Brain Mol. Endocrinol. 8 1994 1298 1308
    • (1994) Mol. Endocrinol. , vol.8 , pp. 1298-1308
    • Mountjoy, K.G.1    Mortrud, M.T.2    Low, M.J.3    Simerly, R.B.4    Cone, R.D.5
  • 6
    • 0030764741 scopus 로고    scopus 로고
    • Antagonism of central melanocortin receptors in vitro and in vivo by Agouti-related protein
    • M.M. Ollmann, B.D. Wilson, Y.K. Yang, J.A. Kerns, Y.R. Chen, I. Gantz, and G.S. Barsh Antagonism of central melanocortin receptors in vitro and in vivo by Agouti-related protein Science 278 1997 135 138
    • (1997) Science , vol.278 , pp. 135-138
    • Ollmann, M.M.1    Wilson, B.D.2    Yang, Y.K.3    Kerns, J.A.4    Chen, Y.R.5    Gantz, I.6    Barsh, G.S.7
  • 8
    • 0033577175 scopus 로고    scopus 로고
    • Long-term administration of MC4 receptor antagonist HS014 causes hyperphagia and obesity in rats
    • A. Kask, R. Pahkla, A. Irs, L. Rago, J.E.S. Wikberg, and H.B. Schioth Long-term administration of MC4 receptor antagonist HS014 causes hyperphagia and obesity in rats Neuroreport 10 1999 707 711
    • (1999) Neuroreport , vol.10 , pp. 707-711
    • Kask, A.1    Pahkla, R.2    Irs, A.3    Rago, L.4    Wikberg, J.E.S.5    Schioth, H.B.6
  • 9
    • 0035044397 scopus 로고    scopus 로고
    • The melanocortin melanocyte-stimulating hormone/adrenocorticotropin(4-10) decreases body fat in humans
    • H.L. Fehm, R. Smolnik, W. Kern, G.P. McGregor, U. Bickel, and J. Born The melanocortin melanocyte-stimulating hormone/adrenocorticotropin(4-10) decreases body fat in humans J. Clin. Endocrinol. Metab. 86 2001 1144 1148
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 1144-1148
    • Fehm, H.L.1    Smolnik, R.2    Kern, W.3    McGregor, G.P.4    Bickel, U.5    Born, J.6
  • 12
    • 0035918601 scopus 로고    scopus 로고
    • Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: Identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants
    • C. Haskell-Luevano, R.D. Cone, E.K. Monck, and Y.P. Wan Structure activity studies of the melanocortin-4 receptor by in vitro mutagenesis: Identification of agouti-related protein (AGRP), melanocortin agonist and synthetic peptide antagonist interaction determinants Biochemistry 40 2001 6164 6179
    • (2001) Biochemistry , vol.40 , pp. 6164-6179
    • Haskell-Luevano, C.1    Cone, R.D.2    Monck, E.K.3    Wan, Y.P.4
  • 13
    • 0030057048 scopus 로고    scopus 로고
    • Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating
    • Z.P. Sun, M.H. Akabas, E.H. Goulding, A. Karlin, and S.A. Siegelbaum Exposure of residues in the cyclic nucleotide-gated channel pore: P region structure and function in gating Neuron 16 1996 141 149
    • (1996) Neuron , vol.16 , pp. 141-149
    • Sun, Z.P.1    Akabas, M.H.2    Goulding, E.H.3    Karlin, A.4    Siegelbaum, S.A.5
  • 14
    • 0030021584 scopus 로고    scopus 로고
    • Molecular basis of charge movement in voltage-gated sodium channels
    • N.B. Yang, A.L. George, and R. Horn Molecular basis of charge movement in voltage-gated sodium channels Neuron 16 1996 113 122
    • (1996) Neuron , vol.16 , pp. 113-122
    • Yang, N.B.1    George, A.L.2    Horn, R.3
  • 15
    • 0031033676 scopus 로고    scopus 로고
    • External cysteine residues in the serotonin transporter
    • J.G. Chen, S. LiuChen, and G. Rudnick External cysteine residues in the serotonin transporter Biochemistry 36 1997 1479 1486
    • (1997) Biochemistry , vol.36 , pp. 1479-1486
    • Chen, J.G.1    Liuchen, S.2    Rudnick, G.3
  • 16
    • 0347064342 scopus 로고    scopus 로고
    • Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis
    • A.A. Kulkarni, I.S. Haworth, T. Uchiyama, and V.H.L. Lee Analysis of transmembrane segment 7 of the dipeptide transporter hPepT1 by cysteine-scanning mutagenesis J. Biol. Chem. 278 2003 51833 51840
    • (2003) J. Biol. Chem. , vol.278 , pp. 51833-51840
    • Kulkarni, A.A.1    Haworth, I.S.2    Uchiyama, T.3    Lee, V.H.L.4
  • 17
    • 0028920298 scopus 로고
    • Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method
    • J.A. Javitch, D.Y. Fu, J.Y. Chen, and A. Karlin Mapping the binding-site crevice of the dopamine D2 receptor by the substituted-cysteine accessibility method Neuron 14 1995 825 831
    • (1995) Neuron , vol.14 , pp. 825-831
    • Javitch, J.A.1    Fu, D.Y.2    Chen, J.Y.3    Karlin, A.4
  • 18
    • 0029757635 scopus 로고    scopus 로고
    • Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice
    • D.Y. Fu, J.A. Ballesteros, H. Weinstein, J.Y. Chen, and J.A. Javitch Residues in the seventh membrane-spanning segment of the dopamine D2 receptor accessible in the binding-site crevice Biochemistry 35 1996 11278 11285
    • (1996) Biochemistry , vol.35 , pp. 11278-11285
    • Fu, D.Y.1    Ballesteros, J.A.2    Weinstein, H.3    Chen, J.Y.4    Javitch, J.A.5
  • 19
    • 0028116711 scopus 로고
    • A cysteine residue in the third membrane-spanning segment of the human D2 dopamine receptor is exposed in the binding-site crevice
    • J.A. Javitch, X. Li, J. Kaback, and A. Karlin A cysteine residue in the third membrane-spanning segment of the human D2 dopamine receptor is exposed in the binding-site crevice Proc. Natl. Acad. Sci. USA 91 1994 10355 10359
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10355-10359
    • Javitch, J.A.1    Li, X.2    Kaback, J.3    Karlin, A.4
  • 20
    • 0033061256 scopus 로고    scopus 로고
    • Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: Constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6
    • S.G. Rasmussen, A.D. Jensen, G. Liapakis, P. Ghanouni, J.A. Javitch, and U. Gether Mutation of a highly conserved aspartic acid in the beta2 adrenergic receptor: constitutive activation, structural instability, and conformational rearrangement of transmembrane segment 6 Mol. Pharmacol. 56 1999 175 184
    • (1999) Mol. Pharmacol. , vol.56 , pp. 175-184
    • Rasmussen, S.G.1    Jensen, A.D.2    Liapakis, G.3    Ghanouni, P.4    Javitch, J.A.5    Gether, U.6
  • 21
    • 1542429075 scopus 로고    scopus 로고
    • Evidence for the proximity of the extreme N-terminus of the neurokinin-2 (NK2) tachykinin receptor to cys167 in the putative fourth transmembrane helix
    • N. Bhogal, F.E. Blaney, P.M. Ingley, J. Rees, and J.B.C. Findlay Evidence for the proximity of the extreme N-terminus of the neurokinin-2 (NK2) tachykinin receptor to cys167 in the putative fourth transmembrane helix Biochemistry 43 2004 3027 3038
    • (2004) Biochemistry , vol.43 , pp. 3027-3038
    • Bhogal, N.1    Blaney, F.E.2    Ingley, P.M.3    Rees, J.4    Findlay, J.B.C.5
  • 22
    • 0141992171 scopus 로고    scopus 로고
    • A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors
    • S. Al-Sabah, and D. Donnelly A model for receptor-peptide binding at the glucagon-like peptide-1 (GLP-1) receptor through the analysis of truncated ligands and receptors Br. J. Pharmacol. 140 2003 339 346
    • (2003) Br. J. Pharmacol. , vol.140 , pp. 339-346
    • Al-Sabah, S.1    Donnelly, D.2
  • 23
    • 0029154516 scopus 로고
    • Cyclic Lactam Alpha-Melanotropin Analogs of Ac-Nle(4)- Cyclo Asp(5),D-Phe(7),Lys(10) Alpha-Melanocyte-Stimulating Hormone-(4-10)-Nh2 with Bulky Aromatic-Amino-Acids at Position- 7 Show High Antagonist Potency and Selectivity at Specific Melanocortin Receptors
    • V.J. Hruby, D.S. Lu, S.D. Sharma, A.D. Castrucci, R.A. Kesterson, F.A. Alobeidi, M.E. Hadley, and R.D. Cone Cyclic Lactam Alpha-Melanotropin Analogs of Ac-Nle(4)- Cyclo Asp(5),D-Phe(7),Lys(10) Alpha-Melanocyte-Stimulating Hormone-(4-10)-Nh2 with Bulky Aromatic-Amino-Acids at Position- 7 Show High Antagonist Potency and Selectivity at Specific Melanocortin Receptors J. Med. Chem. 38 1995 3454 3461
    • (1995) J. Med. Chem. , vol.38 , pp. 3454-3461
    • Hruby, V.J.1    Lu, D.S.2    Sharma, S.D.3    Castrucci, A.D.4    Kesterson, R.A.5    Alobeidi, F.A.6    Hadley, M.E.7    Cone, R.D.8
  • 24
    • 0031786114 scopus 로고    scopus 로고
    • Discovery of a novel superpotent and selective melanocortin-4 receptor antagonist (HS024): Evaluation in vitro and in vivo
    • A. Kask, F. Mutulis, R. Muceniece, R. Pahkla, I. Mutule, J.E.S. Wikberg, L. Rago, and H.B. Schioth Discovery of a novel superpotent and selective melanocortin-4 receptor antagonist (HS024): Evaluation in vitro and in vivo Endocrinology 139 1998 5006 5014
    • (1998) Endocrinology , vol.139 , pp. 5006-5014
    • Kask, A.1    Mutulis, F.2    Muceniece, R.3    Pahkla, R.4    Mutule, I.5    Wikberg, J.E.S.6    Rago, L.7    Schioth, H.B.8
  • 26
    • 0346259943 scopus 로고    scopus 로고
    • Metal ion-mediated agonism and agonist enhancement in melanocortin MC1 and MC4 receptors
    • B. Holst, C.E. Elling, and T.W. Schwartz Metal ion-mediated agonism and agonist enhancement in melanocortin MC1 and MC4 receptors J. Biol. Chem. 277 2002 47662 47670
    • (2002) J. Biol. Chem. , vol.277 , pp. 47662-47670
    • Holst, B.1    Elling, C.E.2    Schwartz, T.W.3
  • 27
    • 0034815978 scopus 로고    scopus 로고
    • Cysteine residues are involved in structure and function of melanocortin 1 receptor: Substitution of a cysteine residue in transmembrane segment two converts an agonist to antagonist
    • P.A. Frandberg, M. Doufexis, S. Kapas, and V. Chhajlani Cysteine residues are involved in structure and function of melanocortin 1 receptor: Substitution of a cysteine residue in transmembrane segment two converts an agonist to antagonist Biochem. Biophys. Res. Commun. 281 2001 851 857
    • (2001) Biochem. Biophys. Res. Commun. , vol.281 , pp. 851-857
    • Frandberg, P.A.1    Doufexis, M.2    Kapas, S.3    Chhajlani, V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.