메뉴 건너뛰기




Volumn 21, Issue 1-2, 2010, Pages 37-55

Analysis of hydrophobic interactions of antagonists with the beta2-adrenergic receptor

Author keywords

Beta adrenoceptor; G protein coupled receptors; Molecular hydrophobicity potential; Protein ligand interactions

Indexed keywords

CRYSTAL STRUCTURE; DISSOCIATION; HYDROPHOBICITY; PHYSIOLOGICAL MODELS; PROTEINS;

EID: 77951434707     PISSN: 1062936X     EISSN: 1029046X     Source Type: Journal    
DOI: 10.1080/10629360903560637     Document Type: Article
Times cited : (8)

References (48)
  • 1
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • R. Fredriksson and H.B. Schioth, The repertoire of G-protein-coupled receptors in fully sequenced genomes, Mol. Pharmacol. 67 (2005), pp. 1414-1425.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schioth, H.B.2
  • 6
    • 0014194186 scopus 로고
    • Differentiation of receptor systems activated by sympathomimetic amines
    • A.M. Lands, A. Arnold, J.P. MacAuliff, and T.G. Brown, Differentiation of receptor systems activated by sympathomimetic amines, Nature 214 (1967), pp. 597-598.
    • (1967) Nature , vol.214 , pp. 597-598
    • Lands, A.M.1    Arnold, A.2    Macauliff, J.P.3    Brown, T.G.4
  • 7
    • 0018607313 scopus 로고
    • Fundamental difference between the molecular interactions of agonists and antagonists with the beta-adrenergic receptor
    • G.A. Weiland, K.P. Minneman, and P.B. Molinoff, Fundamental difference between the molecular interactions of agonists and antagonists with the beta-adrenergic receptor, Nature 281 (1979), pp. 114-117.
    • (1979) Nature , vol.281 , pp. 114-117
    • Weiland, G.A.1    Minneman, K.P.2    Molinoff, P.B.3
  • 8
    • 0022964790 scopus 로고
    • The binding of agonists and antagonists to rat lung beta-adrenergic receptors as investigated by thermodynamics and structure-activity relationships
    • F. Bree, N. el Tayar, H. Van de Waterbeemd, B. Testa, and J.P. Tillement, The binding of agonists and antagonists to rat lung beta-adrenergic receptors as investigated by thermodynamics and structure-activity relationships, J. Recept. Res. 6 (1986), pp. 381-409.
    • (1986) J. Recept. Res. , vol.6 , pp. 381-409
    • Bree, F.1    el Tayar, N.2    van de Waterbeemd, H.3    Testa, B.4    Tillement, J.P.5
  • 9
    • 0022621697 scopus 로고
    • Thermodynamic properties of agonist interactions with the beta-adrenergic receptor-coupled adenylate cyclase system. I. High- and low-affinity states of agonist binding to membrane-bound beta-adrenergic receptors
    • M.L. Contreras, B.B. Wolfe, and P.B. Molinoff, Thermodynamic properties of agonist interactions with the beta-adrenergic receptor-coupled adenylate cyclase system. I. High- and low-affinity states of agonist binding to membrane-bound beta-adrenergic receptors, J. Pharmacol. Exp. Ther. 237 (1986), pp. 154-164.
    • (1986) J. Pharmacol. Exp. Ther. , vol.237 , pp. 154-164
    • Contreras, M.L.1    Wolfe, B.B.2    Molinoff, P.B.3
  • 10
    • 0022641552 scopus 로고
    • Thermodynamic properties of agonist interactions with the beta-adrenergic receptor-coupled adenylate cyclase system. II. Agonist binding to soluble beta-adrenergic receptors
    • M.L. Contreras, B.B. Wolfe, and P.B. Molinoff, Thermodynamic properties of agonist interactions with the beta-adrenergic receptor-coupled adenylate cyclase system. II. Agonist binding to soluble beta-adrenergic receptors, J. Pharmacol. Exp. Ther. 237 (1986), pp. 165-172.
    • (1986) J. Pharmacol. Exp. Ther. , vol.237 , pp. 165-172
    • Contreras, M.L.1    Wolfe, B.B.2    Molinoff, P.B.3
  • 12
    • 14544302297 scopus 로고    scopus 로고
    • The impact of lipophilicity in drug research: A case report on beta-blockers, Mini
    • R. Mannhold, The impact of lipophilicity in drug research: A case report on beta-blockers, Mini Rev. Med. Chem. 5 (2005), pp. 197-205.
    • (2005) Rev. Med. Chem. , vol.5 , pp. 197-205
    • Mannhold, R.1
  • 14
    • 0141992809 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of dopamine 3 (D3) subtype receptor: Discovery of novel and potent D3 ligands through a hybrid pharmacophore- and structure-based database searching approach
    • J. Varady, X. Wu, X. Fang, J. Min, Z. Hu, B. Levant, and S. Wang, Molecular modeling of the three-dimensional structure of dopamine 3 (D3) subtype receptor: Discovery of novel and potent D3 ligands through a hybrid pharmacophore- and structure-based database searching approach, J. Med. Chem. 46 (2003), pp. 4377-4392.
    • (2003) J. Med. Chem. , vol.46 , pp. 4377-4392
    • Varady, J.1    Wu, X.2    Fang, X.3    Min, J.4    Hu, Z.5    Levant, B.6    Wang, S.7
  • 17
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • G. Jones, P. Willett, R.C. Glen, A.R. Leach, and R.D. Taylor, Development and validation of a genetic algorithm for flexible docking, J. Mol. Biol. 267 (1997), pp. 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.D.5
  • 18
    • 76149106701 scopus 로고    scopus 로고
    • version 9.5. Schrödinger, LLC, New York, NY, software
    • MacroModel, version 9.5. Schrödinger, LLC, New York, NY, 2007; software available at http:// www.schrodinger.com
    • (2007) MacroModel
  • 19
    • 0023740863 scopus 로고
    • Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function
    • C.D. Strader, I.S. Sigal, M.R. Candelore, E. Rands, W.S. Hill, and R.A. Dixon, Conserved aspartic acid residues 79 and 113 of the beta-adrenergic receptor have different roles in receptor function, J. Biol. Chem. 263 (1988), pp. 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
  • 20
    • 0032707029 scopus 로고    scopus 로고
    • Study of interaction between agonists and asn293 in helix VI of human beta(2)-adrenergic receptor
    • H.M. Zuurmond, J. Hessling, K. Bluml, M. Lohse, and A.P. Ijzerman, Study of interaction between agonists and asn293 in helix VI of human beta(2)-adrenergic receptor, Mol. Pharmacol. 56 (1999), pp. 909-916.
    • (1999) Mol. Pharmacol , vol.56 , pp. 909-916
    • Zuurmond, H.M.1    Hessling, J.2    Bluml, K.3    Lohse, M.4    Ijzerman, A.P.5
  • 21
    • 33947356279 scopus 로고    scopus 로고
    • G protein coupled receptor structure and activation
    • B.K. Kobilka, G protein coupled receptor structure and activation, Biochim. Biophys. Acta. 1768(2007), pp.794-807.
    • (2007) Biochim. Biophys. Acta. , vol.1768 , pp. 794-807
    • Kobilka, B.K.1
  • 22
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • M.D. Eldridge, C.W. Murray, T.R. Auton, G.V. Paolini, and R.P. Mee, Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes, J. Comp.-Aided Molec. Des. 11 (1997), pp. 425-445.
    • (1997) J. Comp.-Aided Molec. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolini, G.V.4    Mee, R.P.5
  • 23
    • 85195066401 scopus 로고    scopus 로고
    • version 4.5. Schrodinger, LLC, New York, NY, software
    • Glide, version 4.5. Schrodinger, LLC, New York, NY, 2007; software available at http:// www.schrodinger.com
    • (2007) Glide
  • 24
    • 0028411658 scopus 로고
    • Molecular lipophilicity potential, a tool in 3D QSAR: Method and applications
    • P. Gaillard, P.A. Carrupt, B. Testa, and A. Boudon, Molecular lipophilicity potential, a tool in 3D QSAR: Method and applications, J. Comput.-Aided Mol. Des. 8 (1994), pp. 83-96.
    • (1994) J. Comput.-Aided Mol. Des. , vol.8 , pp. 83-96
    • Gaillard, P.1    Carrupt, P.A.2    Testa, B.3    Boudon, A.4
  • 26
    • 0000381930 scopus 로고    scopus 로고
    • Prediction of hydrophobic (lipophilic) properties of small organic molecules using fragmental methods: An analysis of ALOGP and CLOGP methods
    • A.K. Ghose, V.N. Viswanadhan, and J.J. Wendoloski, Prediction of hydrophobic (lipophilic) properties of small organic molecules using fragmental methods: An analysis of ALOGP and CLOGP methods, J. Phys. Chem. 102 (1998), pp. 3762-3772.
    • (1998) J. Phys. Chem. , vol.102 , pp. 3762-3772
    • Ghose, A.K.1    Viswanadhan, V.N.2    Wendoloski, J.J.3
  • 27
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • M.L. Connolly, Solvent-accessible surfaces of proteins and nucleic acids, Science 221 (1983), pp. 709-713.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 28
    • 65449186590 scopus 로고    scopus 로고
    • PLATINUM: A web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes
    • T.V. Pyrkov, A.O. Chugunov, N.A. Krylov, D.E. Nolde, and R.G. Efremov, PLATINUM: A web tool for analysis of hydrophobic/hydrophilic organization of biomolecular complexes, Bioinformatics 25 (2009), pp. 1201-1202.
    • (2009) Bioinformatics , vol.25 , pp. 1201-1202
    • Pyrkov, T.V.1    Chugunov, A.O.2    Krylov, N.A.3    Nolde, D.E.4    Efremov, R.G.5
  • 29
    • 36849001330 scopus 로고    scopus 로고
    • A fragment-based scoring function to re-rank ATP docking results
    • T.V. Pyrkov and R.G. Efremov, A fragment-based scoring function to re-rank ATP docking results, Int. J. Mol. Sci. 8 (2007), pp. 1083-1094.
    • (2007) Int. J. Mol. Sci. , vol.8 , pp. 1083-1094
    • Pyrkov, T.V.1    Efremov, R.G.2
  • 30
    • 0017295075 scopus 로고
    • Beta-Adrenergic receptor interactions. Direct comparison of receptor interaction and biological activity
    • E.M. Brown, S.A. Fedak, C.J. Woodard, and G.D. Aurbach, Beta-Adrenergic receptor interactions. Direct comparison of receptor interaction and biological activity, J. Biol. Chem. 251 (1976), pp. 1239-1246.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1239-1246
    • Brown, E.M.1    Fedak, S.A.2    Woodard, C.J.3    Aurbach, G.D.4
  • 31
    • 0019395308 scopus 로고
    • Characterization of [3H](+/-) carazolol binding to beta-adrenergic receptors
    • A.S. Manalan, H.R. Besch Jr, and A.M. Watanabe, Characterization of [3H](+/-) carazolol binding to beta-adrenergic receptors, Circ. Res. 49 (1981), pp. 326-336.
    • (1981) Circ. Res. , vol.49 , pp. 326-336
    • Manalan, A.S.1    Besch Jr., H.R.2    Watanabe, A.M.3
  • 32
    • 0022212782 scopus 로고
    • Quantitative evaluation of the beta 2-adrenoceptor affinity of phenoxypropanolamines and phenylethanolamines
    • A.P. Ijzerman, G.H. Aue, T. Bultsma, M.R. Linschoten, and H. Timmerman, Quantitative evaluation of the beta 2-adrenoceptor affinity of phenoxypropanolamines and phenylethanolamines, J. Med. Chem. 28 (1985), pp. 1328-1334.
    • (1985) J. Med. Chem. , vol.28 , pp. 1328-1334
    • Ijzerman, A.P.1    Aue, G.H.2    Bultsma, T.3    Linschoten, M.R.4    Timmerman, H.5
  • 33
    • 0036968988 scopus 로고    scopus 로고
    • Mutations inducing divergent shifts of constitutive activity reveal different modes of binding among catecholamine analogues to the beta(2)-adrenergic receptor
    • R. Del Carmine, C. Ambrosio, M. Sbraccia, S. Cotecchia, A.P. Ijzerman, and T. Costa, Mutations inducing divergent shifts of constitutive activity reveal different modes of binding among catecholamine analogues to the beta(2)-adrenergic receptor, Br. J. Pharmacol. 135 (2002), pp. 1715-1722.
    • (2002) Br. J. Pharmacol , vol.135 , pp. 1715-1722
    • Del Carmine, R.1    Ambrosio, C.2    Sbraccia, M.3    Cotecchia, S.4    Ijzerman, A.P.5    Costa, T.6
  • 34
    • 14644421602 scopus 로고    scopus 로고
    • The selectivity of beta-adrenoceptor antagonists at the human beta1, beta2 and beta3 adrenoceptors
    • J.G. Baker, The selectivity of beta-adrenoceptor antagonists at the human beta1, beta2 and beta3 adrenoceptors, Br. J. Pharmacol. 144 (2005), pp. 317-322.
    • (2005) Br. J. Pharmacol. , vol.144 , pp. 317-322
    • Baker, J.G.1
  • 36
    • 67650239912 scopus 로고    scopus 로고
    • Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes
    • V. Katritch, K.A. Reynolds, V. Cherezov, M.A. Hanson, C.B. Roth, M. Yeager, and R. Abagyan, Analysis of full and partial agonists binding to beta2-adrenergic receptor suggests a role of transmembrane helix V in agonist-specific conformational changes, J. Mol. Recognit. 22 (2009), pp. 307-318.
    • (2009) J. Mol. Recognit. , vol.22 , pp. 307-318
    • Katritch, V.1    Reynolds, K.A.2    Cherezov, V.3    Hanson, M.A.4    Roth, C.B.5    Yeager, M.6    Abagyan, R.7
  • 37
    • 0027296745 scopus 로고
    • Amino acid substitutions at position 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modify ligand-binding specificity
    • S. Suryanarayana and B.K. Kobilka, Amino acid substitutions at position 312 in the seventh hydrophobic segment of the beta 2-adrenergic receptor modify ligand-binding specificity, Mol. Pharmacol. 44 (1993), pp. 111-114.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 111-114
    • Suryanarayana, S.1    Kobilka, B.K.2
  • 38
    • 44049086134 scopus 로고    scopus 로고
    • Ligand-stabilized conformational states of human beta(2) adrenergic receptor: Insight into G-protein-coupled receptor activation
    • S. Bhattacharya, S.E. Hal, H. Li, and N. Vaidehi, Ligand-stabilized conformational states of human beta(2) adrenergic receptor: Insight into G-protein-coupled receptor activation, Biophys. J. 94 (2008), pp. 2027-2042.
    • (2008) Biophys. J , vol.94 , pp. 2027-2042
    • Bhattacharya, S.1    Hal, S.E.2    Li, H.3    Vaidehi, N.4
  • 39
    • 0024519931 scopus 로고
    • Structural basis of beta-adrenergic receptor function
    • C.D. Strader, I.S. Sigal, and R.A. Dixon, Structural basis of beta-adrenergic receptor function, FASEB J. 3 (1989), pp. 1825-1832.
    • (1989) FASEB J , vol.3 , pp. 1825-1832
    • Strader, C.D.1    Sigal, I.S.2    Dixon, R.A.3
  • 40
    • 85195032829 scopus 로고    scopus 로고
    • version 8.0. Schrodinger, LLC, New York, NY, software
    • Maestro, version 8.0. Schrodinger, LLC, New York, NY, 2007; software available at http:// www.schrodinger.com
    • (2007) Maestro
  • 41
    • 65049089399 scopus 로고    scopus 로고
    • Identifying conformational changes of the beta(2) adrenoceptor that enable accurate prediction of ligand/receptor interactions and screening for GPCR modulators
    • K.A. Reynolds, V. Katritch, and R. Abagyan, Identifying conformational changes of the beta(2) adrenoceptor that enable accurate prediction of ligand/receptor interactions and screening for GPCR modulators, J. Comput.-Aided Mol. Des. 23 (2009), pp. 273-288.
    • (2009) J. Comput.-Aided Mol. Des. , vol.23 , pp. 273-288
    • Reynolds, K.A.1    Katritch, V.2    Abagyan, R.3
  • 42
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • G. Jones, P. Willett, and R.C. Glen, Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation, J. Mol. Biol. 245 (1995), pp. 43-53.
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 43
    • 0031226772 scopus 로고    scopus 로고
    • Empirical scoring functions: Part 1, the development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes
    • M.D. Eldridge, C.W. Murray, T.R. Auton, G.V. Paolin, and R.P Mee, Empirical scoring functions: Part 1, the development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes, J. Comput.-Aided Mol. Des. 11 (1997), pp. 425-445.
    • (1997) J. Comput.-Aided Mol. Des. , vol.11 , pp. 425-445
    • Eldridge, M.D.1    Murray, C.W.2    Auton, T.R.3    Paolin, G.V.4    Mee, R.P.5
  • 45
    • 77951492953 scopus 로고    scopus 로고
    • version 1.5. Schrodinger, LLC, New York, NY, software
    • CombiGlide, version 1.5. Schrodinger, LLC, New York, NY, 2007; software available at http:// www.schrodinger.com
    • (2007) CombiGlide
  • 47
    • 0036178754 scopus 로고    scopus 로고
    • CoMFA analysis of the human beta(1)-adrenoceptor binding affinity of a series of phenoxypropanolamines
    • S.N. Louis, L.A. Rezmann-Vitti, T.L. Nero, D. Iakovidis, G.P. Jackman, and W.J. Louis, CoMFA analysis of the human beta(1)-adrenoceptor binding affinity of a series of phenoxypropanolamines, Eur. J. Med. Chem. 37 (2002), pp. 111-125.
    • (2002) Eur. J. Med. Chem. , vol.37 , pp. 111-125
    • Louis, S.N.1    Rezmann-Vitti, L.A.2    Nero, T.L.3    Iakovidis, D.4    Jackman, G.P.5    Louis, W.J.6
  • 48
    • 0023735190 scopus 로고
    • Influence of lipophilicity and chirality on the selectivity of ligands for beta 1- and beta 2-adrenoceptors
    • N. el Tayar, B. Testa, H. van de Waterbeemd, P.A. Carrupt, and A.J. Kaumann, Influence of lipophilicity and chirality on the selectivity of ligands for beta 1- and beta 2-adrenoceptors, J. Pharm. Pharmacol. 40 (1988), pp. 609-612.
    • (1988) J. Pharm. Pharmacol. , vol.40 , pp. 609-612
    • el Tayar, N.1    Testa, B.2    van de Waterbeemd, H.3    Carrupt, P.A.4    Kaumann, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.