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Volumn 4, Issue 9, 2009, Pages

Comparative sequence and structural analyses of G-protein-coupled receptor crystal structures and implications for molecular models

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A2 RECEPTOR; BETA 1 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR; CANNABINOID 1 RECEPTOR; CANNABINOID 2 RECEPTOR; CHEMOKINE RECEPTOR CCR5; DOPAMINE 2 RECEPTOR; FOLLITROPIN RECEPTOR; G PROTEIN COUPLED RECEPTOR; LUTEINIZING HORMONE CHORIONIC GONADOTROPIN RECEPTOR; LUTEINIZING HORMONE RECEPTOR; MELANOCORTIN 4 RECEPTOR; MUSCARINIC M1 RECEPTOR; PURINERGIC P2Y1 RECEPTOR; PURINERGIC P2Y12 RECEPTOR; RHODOPSIN; THYROTROPIN RECEPTOR; UNCLASSIFIED DRUG; VASOPRESSIN V1A RECEPTOR; VASOPRESSIN V2 RECEPTOR; DISULFIDE;

EID: 70349513038     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0007011     Document Type: Article
Times cited : (77)

References (87)
  • 1
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • Fredriksson R, Schioth HB (2005) The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol Pharmacol 67: 1414-1425.
    • (2005) Mol Pharmacol , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schioth, H.B.2
  • 3
    • 0033518280 scopus 로고    scopus 로고
    • Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor
    • Liu G, Duranteau L, Carel JC, Monroe J, Doyle DA, et al. (1999) Leydig-cell tumors caused by an activating mutation of the gene encoding the luteinizing hormone receptor. N Engl J Med 341: 1731-1736.
    • (1999) N Engl J Med , vol.341 , pp. 1731-1736
    • Liu, G.1    Duranteau, L.2    Carel, J.C.3    Monroe, J.4    Doyle, D.A.5
  • 4
    • 0031913524 scopus 로고    scopus 로고
    • Activating Smoothened mutations in sporadic basal-cell carcinoma
    • Xie J, Murone M, Luoh SM, Ryan A, Gu Q, et al. (1998) Activating Smoothened mutations in sporadic basal-cell carcinoma. Nature 391: 90-92.
    • (1998) Nature , vol.391 , pp. 90-92
    • Xie, J.1    Murone, M.2    Luoh, S.M.3    Ryan, A.4    Gu, Q.5
  • 5
    • 0026744306 scopus 로고
    • Molecular identification of the gene responsible for congenital nephrogenic diabetes insipidus
    • Rosenthal W, Seibold A, Antaramian A, Lonergan M, Arthus MF, et al. (1992) Molecular identification of the gene responsible for congenital nephrogenic diabetes insipidus. Nature 359: 233-235.
    • (1992) Nature , vol.359 , pp. 233-235
    • Rosenthal, W.1    Seibold, A.2    Antaramian, A.3    Lonergan, M.4    Arthus, M.F.5
  • 6
    • 0027369421 scopus 로고
    • Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas
    • Parma J, Duprez L, Van Sande J, Cochaux P, Gervy C, et al. (1993) Somatic mutations in the thyrotropin receptor gene cause hyperfunctioning thyroid adenomas. Nature 365: 649-651.
    • (1993) Nature , vol.365 , pp. 649-651
    • Parma, J.1    Duprez, L.2    Van Sande, J.3    Cochaux, P.4    Gervy, C.5
  • 7
    • 0041464853 scopus 로고    scopus 로고
    • Ovarian hyperstimulation syndrome due to a mutation in the follicle-stimulating hormone receptor
    • Smits G, Olatunbosun O, Delbaere A, Pierson R, Vassart G, et al. (2003) Ovarian hyperstimulation syndrome due to a mutation in the follicle-stimulating hormone receptor. N Engl J Med 349: 760-766.
    • (2003) N Engl J Med , vol.349 , pp. 760-766
    • Smits, G.1    Olatunbosun, O.2    Delbaere, A.3    Pierson, R.4    Vassart, G.5
  • 8
    • 0041966031 scopus 로고    scopus 로고
    • A chorionic gonadotropin-sensitive mutation in the follicle-stimulating hormone receptor as a cause of familial gestational spontaneous ovarian hyperstimulation syndrome
    • Vasseur C, Rodien P, Beau I, Desroches A, Gérard C, et al. (2003) A chorionic gonadotropin-sensitive mutation in the follicle-stimulating hormone receptor as a cause of familial gestational spontaneous ovarian hyperstimulation syndrome. N Engl J Med 349: 753-759.
    • (2003) N Engl J Med , vol.349 , pp. 753-759
    • Vasseur, C.1    Rodien, P.2    Beau, I.3    Desroches, A.4    Gérard, C.5
  • 9
    • 0027409289 scopus 로고
    • Acquired ocular visual impairment in children. 1960-1989
    • Robinson GC, Jan JE (1993) Acquired ocular visual impairment in children. 1960-1989. Am J Dis Child 147: 325-328.
    • (1993) Am J Dis Child , vol.147 , pp. 325-328
    • Robinson, G.C.1    Jan, J.E.2
  • 10
    • 33646404622 scopus 로고    scopus 로고
    • Melanocortin 4 receptor mutations in a large cohort of severely obese adults: Prevalence, functional classification, genotype-phenotype relationship, and lack of association with binge eating
    • Lubrano-Berthelier C, Dubern B, Lacorte JM, Picard F, Shapiro A, et al. (2006) Melanocortin 4 receptor mutations in a large cohort of severely obese adults: prevalence, functional classification, genotype-phenotype relationship, and lack of association with binge eating. J Clin Endocrinol Metab 91: 1811-1818.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 1811-1818
    • Lubrano-Berthelier, C.1    Dubern, B.2    Lacorte, J.M.3    Picard, F.4    Shapiro, A.5
  • 12
    • 0037020329 scopus 로고    scopus 로고
    • Drug design strategies for targeting G-protein-coupled receptors
    • Klabunde T, Hessler G (2002) Drug design strategies for targeting G-protein-coupled receptors. Chembiochem 3: 928-944.
    • (2002) Chembiochem , vol.3 , pp. 928-944
    • Klabunde, T.1    Hessler, G.2
  • 14
    • 43749109187 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin
    • Murakami M, Kouyama T (2008) Crystal structure of squid rhodopsin. Nature 453: 363-367.
    • (2008) Nature , vol.453 , pp. 363-367
    • Murakami, M.1    Kouyama, T.2
  • 15
  • 16
  • 17
    • 49649086226 scopus 로고    scopus 로고
    • Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region
    • Shimamura T, Hiraki K, Takahashi N, Hori T, Ago H, et al. (2008) Crystal structure of squid rhodopsin with intracellularly extended cytoplasmic region. J Biol Chem 283: 17753-17756.
    • (2008) J Biol Chem , vol.283 , pp. 17753-17756
    • Shimamura, T.1    Hiraki, K.2    Takahashi, N.3    Hori, T.4    Ago, H.5
  • 19
    • 36448995359 scopus 로고    scopus 로고
    • High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor
    • Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, et al. (2007) High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. Science 318: 1258-1265.
    • (2007) Science , vol.318 , pp. 1258-1265
    • Cherezov, V.1    Rosenbaum, D.M.2    Hanson, M.A.3    Rasmussen, S.G.4    Thian, F.S.5
  • 20
    • 36248970132 scopus 로고    scopus 로고
    • Crystal structure of the human beta2 adrenergic G-protein-coupled receptor
    • Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, et al. (2007) Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450: 383-387.
    • (2007) Nature , vol.450 , pp. 383-387
    • Rasmussen, S.G.1    Choi, H.J.2    Rosenbaum, D.M.3    Kobilka, T.S.4    Thian, F.S.5
  • 21
    • 56749103466 scopus 로고    scopus 로고
    • The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist
    • Jaakola VP, Griffith MT, Hanson MA, Cherezov V, Chien EY, et al. (2008) The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist. Science 322: 1211-1217.
    • (2008) Science , vol.322 , pp. 1211-1217
    • Jaakola, V.P.1    Griffith, M.T.2    Hanson, M.A.3    Cherezov, V.4    Chien, E.Y.5
  • 22
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • Park JH, Scheerer P, Hofmann KP, Choe HW, Ernst OP (2008) Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 454: 183-187.
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 23
    • 52949102889 scopus 로고    scopus 로고
    • Crystal structure of opsin in its G-protein-interacting conformation
    • Scheerer P, Park JH, Hildebrand PW, Kim YJ, Krauss N, et al. (2008) Crystal structure of opsin in its G-protein-interacting conformation. Nature 455: 497-502.
    • (2008) Nature , vol.455 , pp. 497-502
    • Scheerer, P.1    Park, J.H.2    Hildebrand, P.W.3    Kim, Y.J.4    Krauss, N.5
  • 24
    • 10644247627 scopus 로고    scopus 로고
    • The third extracellular loop of G-protein-coupled receptors: More than just a linker between two important transmembrane helices
    • Lawson Z, Wheatley M (2004) The third extracellular loop of G-protein-coupled receptors: more than just a linker between two important transmembrane helices. Biochem Soc Trans 32: 1048-1050.
    • (2004) Biochem Soc Trans , vol.32 , pp. 1048-1050
    • Lawson, Z.1    Wheatley, M.2
  • 25
    • 66249144426 scopus 로고    scopus 로고
    • The structure and function of G-protein-coupled receptors
    • Rosenbaum DM, Rasmussen SG, Kobilka BK (2009) The structure and function of G-protein-coupled receptors. Nature 459: 356-363.
    • (2009) Nature , vol.459 , pp. 356-363
    • Rosenbaum, D.M.1    Rasmussen, S.G.2    Kobilka, B.K.3
  • 26
    • 58149203324 scopus 로고    scopus 로고
    • Discovery of New GPCR Biology: One Receptor Structure at a Time
    • Hanson MA, Stevens RC (2009) Discovery of New GPCR Biology: One Receptor Structure at a Time. Structure 17: 8-14.
    • (2009) Structure , vol.17 , pp. 8-14
    • Hanson, M.A.1    Stevens, R.C.2
  • 27
    • 41149160907 scopus 로고    scopus 로고
    • Understanding the structural and functional differences between mouse thyrotropin-releasing hormone receptors 1 and 2
    • Deflorian F, Engel S, Colson AO, Raaka BM, Gershengorn MC, et al. (2008) Understanding the structural and functional differences between mouse thyrotropin-releasing hormone receptors 1 and 2. Proteins 71: 783-794.
    • (2008) Proteins , vol.71 , pp. 783-794
    • Deflorian, F.1    Engel, S.2    Colson, A.O.3    Raaka, B.M.4    Gershengorn, M.C.5
  • 28
    • 67349246265 scopus 로고    scopus 로고
    • Helps to Trace the Molecular Evolution of Class A G-Protein-Coupled Receptors. J Mol Evol
    • Devillé J, Rey J, Chabbert M (2009) An Indel in Transmembrane Helix 2 Helps to Trace the Molecular Evolution of Class A G-Protein-Coupled Receptors. J Mol Evol.
    • (2009) An Indel in Transmembrane Helix , vol.2
    • Devillé, J.1    Rey, J.2    Chabbert, M.3
  • 29
    • 57649105479 scopus 로고    scopus 로고
    • Improved yield of a ligand-binding GPCR expressed in E. coli for structural studies
    • Attrill H, Harding PJ, Smith E, Ross S, Watts A (2009) Improved yield of a ligand-binding GPCR expressed in E. coli for structural studies. Protein Expr Purif 64: 32-38.
    • (2009) Protein Expr Purif , vol.64 , pp. 32-38
    • Attrill, H.1    Harding, P.J.2    Smith, E.3    Ross, S.4    Watts, A.5
  • 31
    • 0033981032 scopus 로고    scopus 로고
    • Molecular and conformational features of a transport-relevant domain in the C-terminal tail of the vasopressin V(2) receptor
    • Krause G, Hermosilla R, Oksche A, Rutz C, Rosenthal W, et al. (2000) Molecular and conformational features of a transport-relevant domain in the C-terminal tail of the vasopressin V(2) receptor. Mol Pharmacol 57: 232-242.
    • (2000) Mol Pharmacol , vol.57 , pp. 232-242
    • Krause, G.1    Hermosilla, R.2    Oksche, A.3    Rutz, C.4    Rosenthal, W.5
  • 32
    • 27544491916 scopus 로고    scopus 로고
    • Characterization of determinants of ligand binding to the nicotinic acid receptor GPR109A (HM74A/PUMA-G)
    • Tunaru S, Lattig J, Kero J, Krause G, Offermanns S (2005) Characterization of determinants of ligand binding to the nicotinic acid receptor GPR109A (HM74A/PUMA-G). Mol Pharmacol 68: 1271-1280.
    • (2005) Mol Pharmacol , vol.68 , pp. 1271-1280
    • Tunaru, S.1    Lattig, J.2    Kero, J.3    Krause, G.4    Offermanns, S.5
  • 33
    • 67849103946 scopus 로고    scopus 로고
    • Structural determinants for selective recognition of peptide ligands for endothelin receptor subtypes ETA and ETB
    • Lattig J, Oksche A, Beyermann M, Rosenthal W, Krause G (2009) Structural determinants for selective recognition of peptide ligands for endothelin receptor subtypes ETA and ETB. J Pept Sci 15: 479-491.
    • (2009) J Pept Sci , vol.15 , pp. 479-491
    • Lattig, J.1    Oksche, A.2    Beyermann, M.3    Rosenthal, W.4    Krause, G.5
  • 34
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • Fredriksson R, Lagerstrom MC, Lundin LG, Schioth HB (2003) The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol 63: 1256-1272.
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4
  • 36
    • 63849294621 scopus 로고    scopus 로고
    • Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations
    • Dror RO, Arlow DH, Borhani DW, Jensen MO, Piana S, et al. (2009) Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations. Proc Natl Acad Sci U S A 106: 4689-4694.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 4689-4694
    • Dror, R.O.1    Arlow, D.H.2    Borhani, D.W.3    Jensen, M.O.4    Piana, S.5
  • 37
    • 0033927916 scopus 로고    scopus 로고
    • Melanocortin-4 receptor mutations are a frequent and heterogeneous cause of morbid obesity
    • Vaisse C, Clement K, Durand E, Hercberg S, Guy-Grand B, et al. (2000) Melanocortin-4 receptor mutations are a frequent and heterogeneous cause of morbid obesity. J Clin Invest 106: 253-262.
    • (2000) J Clin Invest , vol.106 , pp. 253-262
    • Vaisse, C.1    Clement, K.2    Durand, E.3    Hercberg, S.4    Guy-Grand, B.5
  • 38
    • 0037927578 scopus 로고    scopus 로고
    • Poor cell surface expression of human melanocortin-4 receptor mutations associated with obesity
    • Nijenhuis WA, Garner KM, van Rozen RJ, Adan RA (2003) Poor cell surface expression of human melanocortin-4 receptor mutations associated with obesity. J Biol Chem 278: 22939-22945.
    • (2003) J Biol Chem , vol.278 , pp. 22939-22945
    • Nijenhuis, W.A.1    Garner, K.M.2    van Rozen, R.J.3    Adan, R.A.4
  • 39
    • 33645923385 scopus 로고    scopus 로고
    • A supersecondary structure library and search algorithm for modeling loops in protein structures
    • Fernandez-Fuentes N, Oliva B, Fiser As (2006) A supersecondary structure library and search algorithm for modeling loops in protein structures. Nucleic Acids Res 34: 2085-2097.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2085-2097
    • Fernandez-Fuentes, N.1    Oliva, B.2    Fiser, A.3
  • 40
    • 1442310610 scopus 로고    scopus 로고
    • Loops In Proteins (LIP)-a comprehensive loop database for homology modelling
    • Michalsky E, Goede A, Preissner R (2003) Loops In Proteins (LIP)-a comprehensive loop database for homology modelling. Protein Eng 16: 979-985.
    • (2003) Protein Eng , vol.16 , pp. 979-985
    • Michalsky, E.1    Goede, A.2    Preissner, R.3
  • 41
    • 43949095157 scopus 로고    scopus 로고
    • On the applicability of GPCR homology models to computer-aided drug discovery: A comparison between in silico and crystal structures of the beta2-adrenergic receptor
    • Costanzi S (2008) On the applicability of GPCR homology models to computer-aided drug discovery: a comparison between in silico and crystal structures of the beta2-adrenergic receptor. J Med Chem 51: 2907-2914.
    • (2008) J Med Chem , vol.51 , pp. 2907-2914
    • Costanzi, S.1
  • 42
    • 0035450601 scopus 로고    scopus 로고
    • Adaptation to blockade of human immunodeficiency virus type 1 entry imposed by the anti-CCR5 monoclonal antibody 2D7
    • Aarons EJ, Beddows S, Willingham T, Wu L, Koup RA (2001) Adaptation to blockade of human immunodeficiency virus type 1 entry imposed by the anti-CCR5 monoclonal antibody 2D7. Virology 287: 382-390.
    • (2001) Virology , vol.287 , pp. 382-390
    • Aarons, E.J.1    Beddows, S.2    Willingham, T.3    Wu, L.4    Koup, R.A.5
  • 43
    • 0031984539 scopus 로고    scopus 로고
    • Amino-terminal substitutions in the CCR5 coreceptor impair gp120 binding and human immunodeficiency virus type 1 entry
    • Dragic T, Trkola A, Lin SW, Nagashima KA, Kajumo F, et al. (1998) Amino-terminal substitutions in the CCR5 coreceptor impair gp120 binding and human immunodeficiency virus type 1 entry. J Virol 72: 279-285.
    • (1998) J Virol , vol.72 , pp. 279-285
    • Dragic, T.1    Trkola, A.2    Lin, S.W.3    Nagashima, K.A.4    Kajumo, F.5
  • 44
    • 0033515588 scopus 로고    scopus 로고
    • Epitope mapping of CCR5 reveals multiple conformational states and distinct but overlapping structures involved in chemokine and coreceptor function
    • Lee B, Sharron M, Blanpain C, Doranz BJ, Vakili J, et al. (1999) Epitope mapping of CCR5 reveals multiple conformational states and distinct but overlapping structures involved in chemokine and coreceptor function. J Biol Chem 274: 9617-9626.
    • (1999) J Biol Chem , vol.274 , pp. 9617-9626
    • Lee, B.1    Sharron, M.2    Blanpain, C.3    Doranz, B.J.4    Vakili, J.5
  • 45
    • 1542572125 scopus 로고    scopus 로고
    • Mutationally induced disulfide bond formation within the third extracellular loop causes melanocortin 4 receptor inactivation in patients with obesity
    • Tarnow P, Schoneberg T, Krude H, Gruters A, Biebermann H (2003) Mutationally induced disulfide bond formation within the third extracellular loop causes melanocortin 4 receptor inactivation in patients with obesity. J Biol Chem 278: 48666-48673.
    • (2003) J Biol Chem , vol.278 , pp. 48666-48673
    • Tarnow, P.1    Schoneberg, T.2    Krude, H.3    Gruters, A.4    Biebermann, H.5
  • 46
    • 64849104865 scopus 로고    scopus 로고
    • Bellot G, Granier S_TIA, Bourguet W, Seyer R, Rahmeh R, et al. (2009) Structure of the Third Intracellular Loop of the Vasopressin V2 Receptor and Conformational Changes upon Binding to gC1qR. J Mol Biol.
    • Bellot G, Granier S_TIA, Bourguet W, Seyer R, Rahmeh R, et al. (2009) Structure of the Third Intracellular Loop of the Vasopressin V2 Receptor and Conformational Changes upon Binding to gC1qR. J Mol Biol.
  • 47
    • 33846302070 scopus 로고    scopus 로고
    • The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors
    • Pardo L, Deupi X, Dölker N, Lopez R, Campillo M (2007) The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors. Chembiochem 8: 19-24.
    • (2007) Chembiochem , vol.8 , pp. 19-24
    • Pardo, L.1    Deupi, X.2    Dölker, N.3    Lopez, R.4    Campillo, M.5
  • 48
    • 66649096395 scopus 로고    scopus 로고
    • Angel TE, Chance MR, Palczewski K (2009) Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors. Proc Natl Acad Sci U S A.
    • Angel TE, Chance MR, Palczewski K (2009) Conserved waters mediate structural and functional activation of family A (rhodopsin-like) G protein-coupled receptors. Proc Natl Acad Sci U S A.
  • 49
    • 67649203613 scopus 로고    scopus 로고
    • A Heterozygous Mutation in the Third Transmembrane Domain Causes a Dominant-Negative Effect on Signalling Capability of the MC4R
    • Tarnow P, Rediger A, Brumm H, Ambrugger P, Rettenbacher E, et al. (2008) A Heterozygous Mutation in the Third Transmembrane Domain Causes a Dominant-Negative Effect on Signalling Capability of the MC4R. Obesity Facts 1: 155-162.
    • (2008) Obesity Facts , vol.1 , pp. 155-162
    • Tarnow, P.1    Rediger, A.2    Brumm, H.3    Ambrugger, P.4    Rettenbacher, E.5
  • 51
    • 0742288411 scopus 로고    scopus 로고
    • The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors
    • Yohannan S, Faham S, Yang D, Whitelegge JP, Bowie JU (2004) The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptors. Proc Natl Acad Sci U S A 101: 959-963.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 959-963
    • Yohannan, S.1    Faham, S.2    Yang, D.3    Whitelegge, J.P.4    Bowie, J.U.5
  • 52
    • 0036314934 scopus 로고    scopus 로고
    • Structural mimicry of proline kinks: Tertiary packing interactions support local structural distortions
    • Ceruso MA, Weinstein H (2002) Structural mimicry of proline kinks: tertiary packing interactions support local structural distortions. J Mol Biol 318: 1237-1249.
    • (2002) J Mol Biol , vol.318 , pp. 1237-1249
    • Ceruso, M.A.1    Weinstein, H.2
  • 53
    • 76249121106 scopus 로고    scopus 로고
    • Ligand and structure-based models for the prediction of ligand-receptor affinities and virtual screenings: Development and application to the beta(2)-adrenergic receptor
    • June 30 [Epub ahead of print, doi: 10.1002/jcc.21346
    • Vilar S, Karpiak J, Costanzi S (2009) Ligand and structure-based models for the prediction of ligand-receptor affinities and virtual screenings: Development and application to the beta(2)-adrenergic receptor. J Comput Chem 2009 June 30 [Epub ahead of print]. doi: 10.1002/jcc.21346.
    • (2009) J Comput Chem 2009
    • Vilar, S.1    Karpiak, J.2    Costanzi, S.3
  • 54
    • 68149170127 scopus 로고    scopus 로고
    • Neumann S, Huang W, Titus S, Krause G, Kleinau G, et al. (2009) Small Molecule Agonists for the Thyrotropin Receptor Stimulate Thyroid Function in Human Thyrocytes and Mice. Proc Natl Acad Sci U S A.
    • Neumann S, Huang W, Titus S, Krause G, Kleinau G, et al. (2009) Small Molecule Agonists for the Thyrotropin Receptor Stimulate Thyroid Function in Human Thyrocytes and Mice. Proc Natl Acad Sci U S A.
  • 55
    • 0033794067 scopus 로고    scopus 로고
    • Molecular analysis of beta(2)-adrenoceptor coupling to G(s)-, G(i)-, and G(q)-proteins
    • Wenzel-Seifert K, Seifert R (2000) Molecular analysis of beta(2)-adrenoceptor coupling to G(s)-, G(i)-, and G(q)-proteins. Mol Pharmacol 58: 954-966.
    • (2000) Mol Pharmacol , vol.58 , pp. 954-966
    • Wenzel-Seifert, K.1    Seifert, R.2
  • 56
    • 67649743779 scopus 로고    scopus 로고
    • Scheerer P, Heck M, Goede A, Park JH, Choe HW, et al. (2009) Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface. Proc Natl Acad Sci U S A.
    • Scheerer P, Heck M, Goede A, Park JH, Choe HW, et al. (2009) Structural and kinetic modeling of an activating helix switch in the rhodopsin-transducin interface. Proc Natl Acad Sci U S A.
  • 57
    • 56549103329 scopus 로고    scopus 로고
    • Molecular and structural effects of inverse agonistic mutations on signaling of the thyrotropin receptor-a basally active GPCR
    • Kleinau G, Jaeschke H, Mueller S, Worth CL, Paschke R, et al. (2008) Molecular and structural effects of inverse agonistic mutations on signaling of the thyrotropin receptor-a basally active GPCR. Cell Mol Life Sci 65: 3664-3676.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3664-3676
    • Kleinau, G.1    Jaeschke, H.2    Mueller, S.3    Worth, C.L.4    Paschke, R.5
  • 58
    • 66249143720 scopus 로고    scopus 로고
    • Revisiting automated G-protein coupled receptor modeling: The benefit of additional template structures for a neurokinin-1 receptor model
    • Kneissl B, Leonhardt B, Hildebrandt A, Tautermann CS (2009) Revisiting automated G-protein coupled receptor modeling: the benefit of additional template structures for a neurokinin-1 receptor model. J Med Chem 52: 3166-3173.
    • (2009) J Med Chem , vol.52 , pp. 3166-3173
    • Kneissl, B.1    Leonhardt, B.2    Hildebrandt, A.3    Tautermann, C.S.4
  • 59
    • 67349088738 scopus 로고    scopus 로고
    • Michino M, Abola E, Participants GD, Brooks CL, III, Dixon JS, et al. (2009) Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008. Nat Rev Drug Discov.
    • Michino M, Abola E, Participants GD, Brooks CL, III, Dixon JS, et al. (2009) Community-wide assessment of GPCR structure modelling and ligand docking: GPCR Dock 2008. Nat Rev Drug Discov.
  • 60
    • 33846631365 scopus 로고    scopus 로고
    • Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource
    • Kleinau G, Brehm M, Wiedemann U, Labudde D, Leser U, et al. (2007) Implications for molecular mechanisms of glycoprotein hormone receptors using a new sequence-structure-function analysis resource. Mol Endocrinol 21: 574-580.
    • (2007) Mol Endocrinol , vol.21 , pp. 574-580
    • Kleinau, G.1    Brehm, M.2    Wiedemann, U.3    Labudde, D.4    Leser, U.5
  • 63
    • 33846978093 scopus 로고    scopus 로고
    • Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor
    • Kleinau G, Claus M, Jaeschke H, Mueller S, Neumann S, et al. (2007) Contacts between extracellular loop two and transmembrane helix six determine basal activity of the thyroid-stimulating hormone receptor. J Biol Chem 282: 518-525.
    • (2007) J Biol Chem , vol.282 , pp. 518-525
    • Kleinau, G.1    Claus, M.2    Jaeschke, H.3    Mueller, S.4    Neumann, S.5
  • 65
    • 38549097071 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt)
    • The UniProt Consortium
    • The UniProt Consortium (2008) The Universal Protein Resource (UniProt). Nucl Acids Res 36: D190-D195.
    • (2008) Nucl Acids Res , vol.36
  • 66
    • 77957055780 scopus 로고
    • Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relationships in G-Protein Coupled Receptors
    • Ballesteros JA, Weinstein H (1995) Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relationships in G-Protein Coupled Receptors. Methods Neurosci 25: 366-428.
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 67
    • 36448991500 scopus 로고    scopus 로고
    • Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, et al, 2007 Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948
    • Larkin MA, Blackshields G, Brown NP, Chenna R, McGettigan PA, et al. (2007) Clustal W and Clustal X version 2.0. Bioinformatics 23: 2947-2948.
  • 68
    • 0027317580 scopus 로고
    • Performance evaluation of amino acid substitution matrices
    • Henikoff S, Henikoff JG (1993) Performance evaluation of amino acid substitution matrices. Proteins 17: 49-61.
    • (1993) Proteins , vol.17 , pp. 49-61
    • Henikoff, S.1    Henikoff, J.G.2
  • 69
    • 0000009443 scopus 로고    scopus 로고
    • Rapid comparison of protein structures
    • McLachlan A (2009) Rapid comparison of protein structures. Acta Crystallographica Section A 38: 871-873.
    • (2009) Acta Crystallographica Section A , vol.38 , pp. 871-873
    • McLachlan, A.1
  • 70
    • 50149116588 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in bovine rhodopsin: Insight into activation of G-protein-coupled receptors
    • Bhattacharya S, Hall SE, Vaidehi N (2008) Agonist-induced conformational changes in bovine rhodopsin: insight into activation of G-protein-coupled receptors. J Mol Biol 382: 539-555.
    • (2008) J Mol Biol , vol.382 , pp. 539-555
    • Bhattacharya, S.1    Hall, S.E.2    Vaidehi, N.3
  • 71
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor
    • Gether U, Lin S, Ghanouni P, Ballesteros JA, Weinstein H, et al. (1997) Agonists induce conformational changes in transmembrane domains III and VI of the beta2 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
  • 72
    • 0035336676 scopus 로고    scopus 로고
    • Activation of rhodopsin: New insights from structural and biochemical studies
    • Okada T, Ernst OP, Palczewski K, Hofmann KP (2001) Activation of rhodopsin: new insights from structural and biochemical studies. Trends Biochem Sci 26: 318-324.
    • (2001) Trends Biochem Sci , vol.26 , pp. 318-324
    • Okada, T.1    Ernst, O.P.2    Palczewski, K.3    Hofmann, K.P.4
  • 73
    • 0028237927 scopus 로고
    • Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with autosomal dominant retinitis pigmentosa
    • Fuchs S, Kranich H, Denton MJ, Zrenner E, Bhattacharya SS, et al. (1994) Three novel rhodopsin mutations (C110F, L131P, A164V) in patients with autosomal dominant retinitis pigmentosa. Hum Mol Genet 3: 1203.
    • (1994) Hum Mol Genet , vol.3 , pp. 1203
    • Fuchs, S.1    Kranich, H.2    Denton, M.J.3    Zrenner, E.4    Bhattacharya, S.S.5
  • 74
    • 59649112109 scopus 로고    scopus 로고
    • Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation
    • Ahuja S, Hornak V, Yan EC, Syrett N, Goncalves JA, et al. (2009) Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation. Nat Struct Mol Biol 16: 168-175.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 168-175
    • Ahuja, S.1    Hornak, V.2    Yan, E.C.3    Syrett, N.4    Goncalves, J.A.5
  • 77
    • 0028125886 scopus 로고
    • Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness
    • Rao VR, Cohen GB, Oprian DD (1994) Rhodopsin mutation G90D and a molecular mechanism for congenital night blindness. Nature 367: 639-642.
    • (1994) Nature , vol.367 , pp. 639-642
    • Rao, V.R.1    Cohen, G.B.2    Oprian, D.D.3
  • 79
    • 0036932174 scopus 로고    scopus 로고
    • Decreased muscarinic1 receptors in the dorsolateral prefrontal cortex of subjects with schizophrenia
    • Dean B, McLeod M, Keriakous D, McKenzie J, Scarr E (2002) Decreased muscarinic1 receptors in the dorsolateral prefrontal cortex of subjects with schizophrenia. Mol Psychiatry 7: 1083-1091.
    • (2002) Mol Psychiatry , vol.7 , pp. 1083-1091
    • Dean, B.1    McLeod, M.2    Keriakous, D.3    McKenzie, J.4    Scarr, E.5
  • 80
    • 32244447628 scopus 로고    scopus 로고
    • Glatt SJ, Jonsson EG (2006) The Cys allele of the DRD2 Ser311Cys polymorphism has a dominant effect on risk for schizophrenia: evidence from fixed- and random-effects meta-analyses. Am J Med Genet B Neuropsychiatr Genet 141B: 149-154.
    • Glatt SJ, Jonsson EG (2006) The Cys allele of the DRD2 Ser311Cys polymorphism has a dominant effect on risk for schizophrenia: evidence from fixed- and random-effects meta-analyses. Am J Med Genet B Neuropsychiatr Genet 141B: 149-154.
  • 82
    • 58149091678 scopus 로고    scopus 로고
    • Shared and distinct genetic variants in type 1 diabetes and celiac disease
    • Smyth DJ, Plagnol V, Walker NM, Cooper JD, Downes K, et al. (2008) Shared and distinct genetic variants in type 1 diabetes and celiac disease. N Engl J Med 359: 2767-2777.
    • (2008) N Engl J Med , vol.359 , pp. 2767-2777
    • Smyth, D.J.1    Plagnol, V.2    Walker, N.M.3    Cooper, J.D.4    Downes, K.5
  • 83
    • 34347273447 scopus 로고    scopus 로고
    • Genetic variations at the endocannabinoid type 1 receptor gene (CNR1) are associated with obesity phenotypes in men
    • Russo P, Strazzullo P, Cappuccio FP, Tregouet DA, Lauria F, et al. (2007) Genetic variations at the endocannabinoid type 1 receptor gene (CNR1) are associated with obesity phenotypes in men. J Clin Endocrinol Metab 92: 2382-2386.
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 2382-2386
    • Russo, P.1    Strazzullo, P.2    Cappuccio, F.P.3    Tregouet, D.A.4    Lauria, F.5
  • 86
    • 0035843178 scopus 로고    scopus 로고
    • Identification of the platelet ADP receptor targeted by antithrombotic drugs
    • Hollopeter G, Jantzen HM, Vincent D, Li G, England L, et al. (2001) Identification of the platelet ADP receptor targeted by antithrombotic drugs. Nature 409: 202-207.
    • (2001) Nature , vol.409 , pp. 202-207
    • Hollopeter, G.1    Jantzen, H.M.2    Vincent, D.3    Li, G.4    England, L.5
  • 87
    • 0028808086 scopus 로고
    • Activating mutations of the TSH receptor in differentiated thyroid carcinomas
    • Russo D, Arturi F, Schlumberger M, Caillou B, Monier R, et al. (1995) Activating mutations of the TSH receptor in differentiated thyroid carcinomas. Oncogene 11: 1907-1911.
    • (1995) Oncogene , vol.11 , pp. 1907-1911
    • Russo, D.1    Arturi, F.2    Schlumberger, M.3    Caillou, B.4    Monier, R.5


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