메뉴 건너뛰기




Volumn 73, Issue 1, 2008, Pages 173-184

Three-dimensional model of the human urotensin-II receptor: Docking of human urotensin-II and nonpeptide antagonists in the binding site and comparison with an antagonist pharmacophore model

Author keywords

Antagonists; GPCR; GPR14; Molecular modeling; Urotensin II

Indexed keywords

BENZAZEPINE DERIVATIVE; OPIATE ANTAGONIST; PALOSURAN; QUINOLINE DERIVATIVE; UNCLASSIFIED DRUG; UROTENSIN 2 ANTAGONIST; UROTENSIN II;

EID: 50849111783     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22050     Document Type: Article
Times cited : (14)

References (53)
  • 2
    • 0033776533 scopus 로고    scopus 로고
    • Orphan-receptor ligand human urotensin II: Receptor localization in human tissues and comparison of vasoconstrictor responses with endothelin-1
    • Maguire JJ, Kuc EK, Davenport AP. Orphan-receptor ligand human urotensin II: receptor localization in human tissues and comparison of vasoconstrictor responses with endothelin-1. Br J Pharmacol 2000;131:441-446.
    • (2000) Br J Pharmacol , vol.131 , pp. 441-446
    • Maguire, J.J.1    Kuc, E.K.2    Davenport, A.P.3
  • 5
    • 0029102720 scopus 로고
    • Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors
    • Marchese A, Heiber M, Nguyen T, Heng HH, Saldivia VR, Cheng R, Murphy PM, Tsui LC, Shi X, Gregor P. Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors. Genomics 1995;29:335-344.
    • (1995) Genomics , vol.29 , pp. 335-344
    • Marchese, A.1    Heiber, M.2    Nguyen, T.3    Heng, H.H.4    Saldivia, V.R.5    Cheng, R.6    Murphy, P.M.7    Tsui, L.C.8    Shi, X.9    Gregor, P.10
  • 6
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • Mirzadegan T, Benko G, Filipek S, Palczewski K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 2003;42:2759-2767.
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 8
    • 0026438883 scopus 로고
    • Isolation and primary structure of urotensin II from the brain of a tetrapod, the frog Rana ridibunda
    • Conlon JM, O'Harte F, Smith DD, Tonon MC, Vaudry H. Isolation and primary structure of urotensin II from the brain of a tetrapod, the frog Rana ridibunda. Biochem Biophys Res Commun 1992;188:578-583.
    • (1992) Biochem Biophys Res Commun , vol.188 , pp. 578-583
    • Conlon, J.M.1    O'Harte, F.2    Smith, D.D.3    Tonon, M.C.4    Vaudry, H.5
  • 9
    • 0344549382 scopus 로고    scopus 로고
    • Cloning, sequence analysis and tissue distribution of the mouse and rat urotensin II precursors
    • Coulouarn Y, Jegou S, Tostivint H, Vaudry H, Lihrmann I. Cloning, sequence analysis and tissue distribution of the mouse and rat urotensin II precursors. FEBS Lett 1999;457:28-32.
    • (1999) FEBS Lett , vol.457 , pp. 28-32
    • Coulouarn, Y.1    Jegou, S.2    Tostivint, H.3    Vaudry, H.4    Lihrmann, I.5
  • 10
    • 0034466374 scopus 로고    scopus 로고
    • Human urotensin-II, the most potent mammalian vasoconstrictor identified to date, as a therapeutic target for the management of cardiovascular disease
    • Douglas SA, Ohlstein EH. Human urotensin-II, the most potent mammalian vasoconstrictor identified to date, as a therapeutic target for the management of cardiovascular disease. Trends Cardiovasc Med 2000;10:229-237.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 229-237
    • Douglas, S.A.1    Ohlstein, E.H.2
  • 11
    • 0033638718 scopus 로고    scopus 로고
    • Differential vasoconstrictor activity of human urotensin-II in vascular tissue isolated from the rat, mouse, dog, pig, marmoset and cynomolgus monkey
    • Douglas SA, Sulpizio AC, Piercy V, Sarau HM, Ames RS, Aiyar NV, Ohlstein EH, Willette RN. Differential vasoconstrictor activity of human urotensin-II in vascular tissue isolated from the rat, mouse, dog, pig, marmoset and cynomolgus monkey. Br J Pharmacol 2000;131:1262-1274.
    • (2000) Br J Pharmacol , vol.131 , pp. 1262-1274
    • Douglas, S.A.1    Sulpizio, A.C.2    Piercy, V.3    Sarau, H.M.4    Ames, R.S.5    Aiyar, N.V.6    Ohlstein, E.H.7    Willette, R.N.8
  • 13
  • 14
    • 0032428160 scopus 로고    scopus 로고
    • Cloning of the cDNA encoding the urotensin II precursor in frog and human reveals intense expression of the urotensin II gene in motoneurons of the spinal cord
    • Coulouarn Y, Lihrmann I, Jegou S, Anouar Y, Tostivint H, Beauvillain JC, Conlon JM, Bern HA, Vaudry H. Cloning of the cDNA encoding the urotensin II precursor in frog and human reveals intense expression of the urotensin II gene in motoneurons of the spinal cord. Proc Natl Acad Sci USA 1998;95:15803-15808.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15803-15808
    • Coulouarn, Y.1    Lihrmann, I.2    Jegou, S.3    Anouar, Y.4    Tostivint, H.5    Beauvillain, J.C.6    Conlon, J.M.7    Bern, H.A.8    Vaudry, H.9
  • 16
    • 0037171726 scopus 로고    scopus 로고
    • Identification of nonpeptidic urotensin II receptor antagonists by virtual screening based on a pharmacophore model derived from structure-activity relationships and nuclear magnetic resonance studies on urotensin II
    • Flohr S, Kurz M, Kostenis E, Brkovich A, Fournier A, Klabunde T. Identification of nonpeptidic urotensin II receptor antagonists by virtual screening based on a pharmacophore model derived from structure-activity relationships and nuclear magnetic resonance studies on urotensin II. J Med Chem 2002;45:1799-1805.
    • (2002) J Med Chem , vol.45 , pp. 1799-1805
    • Flohr, S.1    Kurz, M.2    Kostenis, E.3    Brkovich, A.4    Fournier, A.5    Klabunde, T.6
  • 19
    • 20044372934 scopus 로고    scopus 로고
    • Urotensin II: Its function in health and its role in disease
    • Ong KL, Lam KS, Cheung BM. Urotensin II: its function in health and its role in disease. Cardiovasc Drugs Ther 2005;19:65-75.
    • (2005) Cardiovasc Drugs Ther , vol.19 , pp. 65-75
    • Ong, K.L.1    Lam, K.S.2    Cheung, B.M.3
  • 22
    • 50849118642 scopus 로고    scopus 로고
    • Takeda Chemical Industries, Assignee. Preparation of 2,3,4,5-tetrahydro-1H-3-benzazepine derivatives as GPR14 antagonists
    • WO patent 2002002530
    • Tarui N, Santo T, Watanabe H, Aso K, Ishihara Y; Takeda Chemical Industries, Assignee. Preparation of 2,3,4,5-tetrahydro-1H-3-benzazepine derivatives as GPR14 antagonists. WO patent 2002002530. 2002.
    • (2002)
    • Tarui, N.1    Santo, T.2    Watanabe, H.3    Aso, K.4    Ishihara, Y.5
  • 23
    • 50849113626 scopus 로고    scopus 로고
    • Takeda Chemical Industries, Assignee. Quinoline derivatives as vasoactive agents exhibiting orphan receptor GPR14 protein antagonism
    • WO patent 2001066143
    • Tarui N, Santo T, Mori M, Watanabe H; Takeda Chemical Industries, Assignee. Quinoline derivatives as vasoactive agents exhibiting orphan receptor GPR14 protein antagonism. WO patent 2001066143. 2001.
    • (2001)
    • Tarui, N.1    Santo, T.2    Mori, M.3    Watanabe, H.4
  • 24
    • 34247244635 scopus 로고    scopus 로고
    • Lescot E, Sopkova-de Oliveira Santos J, Dubessy C, Oulyadi H, Lesnard A, Vaudry H, Bureau R, Rault S. Definition of news pharmacophores for non-peptide antagonists of human urotensin-II. Comparaison with the 3D-structure of human urotensin-II and URP. J Chem Inf Mod 2007;47:602-612.
    • Lescot E, Sopkova-de Oliveira Santos J, Dubessy C, Oulyadi H, Lesnard A, Vaudry H, Bureau R, Rault S. Definition of news pharmacophores for non-peptide antagonists of human urotensin-II. Comparaison with the 3D-structure of human urotensin-II and URP. J Chem Inf Mod 2007;47:602-612.
  • 25
    • 17144378929 scopus 로고    scopus 로고
    • Architecture of the human urotensin II receptor: Comparison of the binding domains of peptide and non-peptide urotensin II agonists
    • Lavecchia A, Cosconati S, Novellino E. Architecture of the human urotensin II receptor: comparison of the binding domains of peptide and non-peptide urotensin II agonists. J Med Chem 2005;48:2480-2492.
    • (2005) J Med Chem , vol.48 , pp. 2480-2492
    • Lavecchia, A.1    Cosconati, S.2    Novellino, E.3
  • 29
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3D-PSSM
    • Kelley LA, MacCallum RM, Sternberg MJ. Enhanced genome annotation using structural profiles in the program 3D-PSSM. J Mol Biol 2000;299:499-520.
    • (2000) J Mol Biol , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 30
    • 0031680752 scopus 로고    scopus 로고
    • Incremental threading optimization (TITO) to help alignment and modelling of remote homologues
    • Labesse G, Mornon J. Incremental threading optimization (TITO) to help alignment and modelling of remote homologues. Bioinformatics 1998;14:206-211.
    • (1998) Bioinformatics , vol.14 , pp. 206-211
    • Labesse, G.1    Mornon, J.2
  • 31
    • 0027136282 scopus 로고    scopus 로고
    • Sali A, Blundell TL. Comparative protein modelling by satistaction of spatial restraints. Modeller. J Mol Biol 1993;234:779-815.
    • Sali A, Blundell TL. Comparative protein modelling by satistaction of spatial restraints. Modeller. J Mol Biol 1993;234:779-815.
  • 32
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ. Recognition of errors in three-dimensional structures of proteins. Proteins 1993;17:355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 33
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 1992;356:83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 34
    • 0034843745 scopus 로고    scopus 로고
    • Easier threading through web-based comparisons and cross-validations
    • Douguet D, Labesse G. Easier threading through web-based comparisons and cross-validations. Bioinformatics 2001;17:752-753.
    • (2001) Bioinformatics , vol.17 , pp. 752-753
    • Douguet, D.1    Labesse, G.2
  • 35
    • 0036301007 scopus 로고    scopus 로고
    • Bicelle crystallization: A new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure
    • Faham S, Bowie JU. Bicelle crystallization: a new method for crystallizing membrane proteins yields a monomeric bacteriorhodopsin structure. J Mol Biol 2002;316:1-6.
    • (2002) J Mol Biol , vol.316 , pp. 1-6
    • Faham, S.1    Bowie, J.U.2
  • 40
    • 0348059194 scopus 로고    scopus 로고
    • Marvin sketch and Marvin view: Molecule applets for the world wide web
    • editor. Switzerland MDPI;
    • Csizmadia P. Marvin sketch and Marvin view: molecule applets for the world wide web. In: Esteban Pombo-Villar RNaS-KL, editor. Switzerland MDPI; 2000. p. 367-369.
    • (2000) Esteban Pombo-Villar RNaS-KL , pp. 367-369
    • Csizmadia, P.1
  • 41
    • 84986522856 scopus 로고
    • Poling; promoting conformational variation
    • Smellie A, Teig SL, Towin P. Poling; promoting conformational variation. J Comput Chem 1995;16:171-187.
    • (1995) J Comput Chem , vol.16 , pp. 171-187
    • Smellie, A.1    Teig, S.L.2    Towin, P.3
  • 42
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 1995;245:43-53.
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 43
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G, Willett P, Glen RC, Leach AR, Taylor R. Development and validation of a genetic algorithm for flexible docking. J Mol Biol 1997;267:727-748.
    • (1997) J Mol Biol , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 44
    • 50849105601 scopus 로고    scopus 로고
    • Sybyl molecular modeling package, version 7.0, Tripos, St Louis, Mo
    • Sybyl molecular modeling package, version 7.0, Tripos, St Louis, Mo.
  • 45
    • 50849092131 scopus 로고    scopus 로고
    • Case DA, Darden TA, Cheatham I, Simmerling J, Wang RE, Duke R, Luo KM, Merz B, Wang DA, Pearlman M, Crowley M, Brozell S, Tsui V, Gohlke H, Mongan J, Hornak V, Cui G, Beroza P, Schafmeister C, Caldwell JW, Ross WS, Kollman PA. AMBER8. University of California, San Francisco; 2004.
    • Case DA, Darden TA, Cheatham I, Simmerling J, Wang RE, Duke R, Luo KM, Merz B, Wang DA, Pearlman M, Crowley M, Brozell S, Tsui V, Gohlke H, Mongan J, Hornak V, Cui G, Beroza P, Schafmeister C, Caldwell JW, Ross WS, Kollman PA. AMBER8. University of California, San Francisco; 2004.
  • 46
    • 2942722780 scopus 로고    scopus 로고
    • High-throughput modeling of human G-protein coupled receptors: Amino acid sequence alignment, Three-dimensional model building, and receptor library screening
    • Bissantz C, Logean A, Rognan D. High-throughput modeling of human G-protein coupled receptors: amino acid sequence alignment, Three-dimensional model building, and receptor library screening. J Chem Inf Comput Sci 2004;44.
    • (2004) J Chem Inf Comput Sci , pp. 44
    • Bissantz, C.1    Logean, A.2    Rognan, D.3
  • 47
    • 0001552169 scopus 로고    scopus 로고
    • A disulfide bond between conserved cysteines in the extracellular loops of the human VIP receptor is required for binding and activation
    • Knudsen MS, Tams JW, Wulff BS, Fahrenkrug J. A disulfide bond between conserved cysteines in the extracellular loops of the human VIP receptor is required for binding and activation. FEBS Lett 1997;412:141-143.
    • (1997) FEBS Lett , vol.412 , pp. 141-143
    • Knudsen, M.S.1    Tams, J.W.2    Wulff, B.S.3    Fahrenkrug, J.4
  • 48
    • 0035902441 scopus 로고    scopus 로고
    • Identification and function of disulfide bridges in the extracellular domains of the angiotensin II type 2 receptor
    • Heerding JN, Hines J, Fluharty SJ, Yee DK. Identification and function of disulfide bridges in the extracellular domains of the angiotensin II type 2 receptor. Biochemistry 2001;40:8369-8377.
    • (2001) Biochemistry , vol.40 , pp. 8369-8377
    • Heerding, J.N.1    Hines, J.2    Fluharty, S.J.3    Yee, D.K.4
  • 49
    • 0028787944 scopus 로고
    • Identification of a critical aspartate residue in transmembrane domain three necessary for the binding of somatostatin to the somatostatin receptor SSTR2
    • Strnad J, Hadcock JR. Identification of a critical aspartate residue in transmembrane domain three necessary for the binding of somatostatin to the somatostatin receptor SSTR2. Biochem Biophys Res Commun 1995;216:913-921.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 913-921
    • Strnad, J.1    Hadcock, J.R.2
  • 50
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function
    • Strader CD, Sigal IS, Candelore MR, Rands E, Hill WS, Dixon RA. Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function. J Biol Chem 1988;263:10267-10271.
    • (1988) J Biol Chem , vol.263 , pp. 10267-10271
    • Strader, C.D.1    Sigal, I.S.2    Candelore, M.R.3    Rands, E.4    Hill, W.S.5    Dixon, R.A.6
  • 51
    • 33646594152 scopus 로고    scopus 로고
    • Characterization of urotensin-II receptor structural domains involved in the recognition of U-II, URP, and urantide
    • Boivin S, Guilhaudis L, Milazzo I, Oulyadi H, Davoust D, Fournier A. Characterization of urotensin-II receptor structural domains involved in the recognition of U-II, URP, and urantide. Biochemisty 2006;45:5993-6002.
    • (2006) Biochemisty , vol.45 , pp. 5993-6002
    • Boivin, S.1    Guilhaudis, L.2    Milazzo, I.3    Oulyadi, H.4    Davoust, D.5    Fournier, A.6
  • 53
    • 0032546782 scopus 로고    scopus 로고
    • pi-Stacking interactions. Alive and well in proteins
    • McGaughey GB, Gagne M, Rappe AK. pi-Stacking interactions. Alive and well in proteins. J Biol Chem 1998;25:15458-15463.
    • (1998) J Biol Chem , vol.25 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappe, A.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.