메뉴 건너뛰기




Volumn 47, Issue 22, 2004, Pages 5393-5404

Architecture of P2Y nucleotide receptors: Structural comparison based on sequence analysis, mutagenesis, and homology modeling

Author keywords

[No Author keywords available]

Indexed keywords

2 METHYLTHIOADENOSINE DIPHOSPHATE; 2' DEOXY 6 N METHYLADENOSINE 3',5' BISPHOSPHATE; ADENINE NUCLEOTIDE; ALANINE; G PROTEIN COUPLED RECEPTOR; PHENYLALANINE; PURINE P2Y RECEPTOR; PURINE P2Y1 RECEPTOR; PURINE P2Y12 RECEPTOR; PURINERGIC RECEPTOR AFFECTING AGENT; PURINERGIC RECEPTOR BLOCKING AGENT; RHODOPSIN; TYROSINE; UNCLASSIFIED DRUG; URACIL;

EID: 6044234752     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm049914c     Document Type: Article
Times cited : (134)

References (55)
  • 1
    • 0037068428 scopus 로고    scopus 로고
    • Purine and pyrimidine (P2) receptors as drug targets
    • Jacobson, K. A.; Jarvis, M. F.; Williams, M. Purine and Pyrimidine (P2) Receptors as Drug Targets. J. Med. Chem. 2002, 45, 4057-4093.
    • (2002) J. Med. Chem. , vol.45 , pp. 4057-4093
    • Jacobson, K.A.1    Jarvis, M.F.2    Williams, M.3
  • 6
    • 0035800032 scopus 로고    scopus 로고
    • Advances in determination of a high-resolution three-dimensional structure of rhodopsin, a model of G-Protein-Coupled Receptors (GPCRs)
    • (b) Teller, D. C.; Okada, T.; Behnke, C. A.; Palczewski, K.; Stenkamp, R. E. Advances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs). Biochemistry 2001, 40, 7761-7772.
    • (2001) Biochemistry , vol.40 , pp. 7761-7772
    • Teller, D.C.1    Okada, T.2    Behnke, C.A.3    Palczewski, K.4    Stenkamp, R.E.5
  • 8
    • 0035797877 scopus 로고    scopus 로고
    • Studies on the structure of the G protein-coupled receptor rhodopsin including the putative G-Protein binding site in unactivated and activated forms
    • (d) Yeagle, P. L.; Choi, G.; Albert, A. D. Studies on the Structure of the G Protein-Coupled Receptor Rhodopsin Including the Putative G-Protein Binding Site in Unactivated and Activated Forms. Biochemistry 2001, 40, 11932-11937.
    • (2001) Biochemistry , vol.40 , pp. 11932-11937
    • Yeagle, P.L.1    Choi, G.2    Albert, A.D.3
  • 10
    • 0032559887 scopus 로고    scopus 로고
    • 1 receptor: Molecular modeling and site-directed mutagenesis as tools to identify agonist and antagonist recognition sites
    • 1 Receptor: Molecular Modeling and Site-Directed Mutagenesis as Tools to Identify Agonist and Antagonist Recognition Sites. J. Med. Chem. 1998, 41, 1456-1466.
    • (1998) J. Med. Chem. , vol.41 , pp. 1456-1466
    • Moro, S.1    Guo, D.2    Camaioni, E.3    Boyer, J.L.4    Harden, T.K.5    Jacobson, K.A.6
  • 13
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models and computational probing of structure-function relations in G-Protein coupled receptors
    • Ballesteros, J. A.; Weinstein, H. Integrated Methods for the Construction of Three-Dimensional Models and Computational Probing of Structure-Function Relations in G-Protein Coupled Receptors. Methods Neurosci. 1995, 25, 366-428.
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 14
    • 0029919840 scopus 로고    scopus 로고
    • Molecular architecture of G protein-coupled receptors
    • van Rhee, A. M.; Jacobson, K. A. Molecular Architecture of G Protein-Coupled Receptors. Drug Dev. Res. 1996, 37, 1-38.
    • (1996) Drug Dev. Res. , vol.37 , pp. 1-38
    • Van Rhee, A.M.1    Jacobson, K.A.2
  • 15
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D.; Gibson, T. J.; Plewniak, F.; Jeanmougin, F.; Higgins, D. G. The CLUSTAL_X Windows Interface: Flexible Strategies for Multiple Sequence Alignment Aided by Quality Analysis Tools. Nucleic Acids Res. 1997, 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 16
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D.; Higgins, D. G.; Gibson, T. J. CLUSTAL W: Improving the Sensitivity of Progressive Multiple Sequence Alignment Through Sequence Weighting, Position-Specific Gap Penalties and Weight Matrix Choice. Nucleic Acids Res. 1994, 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 17
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N.; Nei, M. The Neighbor-Joining Method: A New Method for Reconstructing Phylogenetic Trees. Mol Biol Evol. 1987, 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 18
    • 0000228203 scopus 로고
    • National Biomedical Research Foundation: Washington, DC
    • Dayhoff, M. O. Atlas of Protein Sequence and Structure; National Biomedical Research Foundation: Washington, DC, 1978; vol. 5, suppl. 3, pp 345-352.
    • (1978) Atlas of Protein Sequence and Structure , vol.5 , Issue.SUPPL. 3 , pp. 345-352
    • Dayhoff, M.O.1
  • 19
    • 0037162029 scopus 로고    scopus 로고
    • Sphingosylphosphorylcholine and lysophosphatidylcholine: G protein-coupled receptors and receptor-mediated signal transduction
    • Xu, Y. Sphingosylphosphorylcholine and Lysophosphatidylcholine: G Protein-Coupled Receptors and Receptor-Mediated Signal Transduction. Biochim. Biophys. Acta 2002, 1582, 81-88.
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 81-88
    • Xu, Y.1
  • 20
    • 0038152846 scopus 로고    scopus 로고
    • Identification of P2y9/GPR23 as novel G protein-coupled receptor for lysophosphatidic acid, structurally distant from the Edg family
    • Noguchi, K.; Ishi, S.; Shimizu, T. Identification of P2y9/GPR23 as Novel G Protein-Coupled Receptor for Lysophosphatidic Acid, Structurally Distant from the Edg Family. J. Biol. Chem. 2003, 278, 25600-25606.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25600-25606
    • Noguchi, K.1    Ishi, S.2    Shimizu, T.3
  • 21
    • 0033613183 scopus 로고    scopus 로고
    • How the protease thrombin talks to cells
    • Coughlin, S. R. How the Protease Thrombin Talks to Cells. Proc. Natl. Acad. Sci. U.S.A. 1999, 96, 11023-11027.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11023-11027
    • Coughlin, S.R.1
  • 23
    • 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, M. C.; Lundin, L. G.; Schioth, H. B. The G-Protein-Coupled Receptors in the Human Genome Form Five Main Families. Phylogenetic Analysis, Paralogon Groups, and Fingerprints. Mol. Pharmacol. 2003, 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
  • 29
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A.; Blundell, T. L. Comparative Protein Modelling by Satisfaction of Spatial Restraints. J. Mol. Biol. 1993, 234, 779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 30
    • 0028051828 scopus 로고
    • Derivation of rules for comparative protein modeling from a database of protein structure alignments
    • Sali, A.; Overington, J. P. Derivation of rules for comparative protein modeling from a database of protein structure alignments. Protein Sci. 1994, 3, 1582-1596.
    • (1994) Protein Sci. , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 31
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S. Thornton. J. M. PROCHECK: A Program to Check the Stereochemical Quality of Protein Structures. J. Appl. Crystallogr. 1993, 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 33
    • 0001008704 scopus 로고
    • Molecular dynamics simulation of a bilayer of 200 lipids in the gel and in the liquid-crystal phases
    • Heller, H.; Schaefer, M.; Schulten, K. Molecular Dynamics Simulation of a Bilayer of 200 Lipids in the Gel and in the Liquid-Crystal Phases. J. Phys. Chem. 1993, 97, 8343-8360.
    • (1993) J. Phys. Chem. , vol.97 , pp. 8343-8360
    • Heller, H.1    Schaefer, M.2    Schulten, K.3
  • 35
    • 84929698191 scopus 로고    scopus 로고
    • 2T) receptor antagonist for the treatment of thrombosis
    • New Orleans, LA, March 23-27
    • 2T) Receptor Antagonist for the Treatment of Thrombosis. 16 MEDI, 225th ACS National Meeting, New Orleans, LA, March 23-27, 2003.
    • (2003) 16 MEDI, 225th ACS National Meeting
    • Springthorpe, B.1
  • 38
    • 0034948696 scopus 로고    scopus 로고
    • Structural mimicry in G protein-coupled receptors: Implications of the high-resolution structure of rhodopsin for structure-function analysis of rhodopsin-like receptors
    • Review
    • Ballesteros, J. A.; Shi, L.; Javitch, J. A. Structural Mimicry in G Protein-Coupled Receptors: Implications of the High-Resolution Structure of Rhodopsin for Structure-Function Analysis of Rhodopsin-like Receptors. Mol. Pharmacol. 2001, 60, 1-19. Review. Erratum in: Mol. Pharmacol. 2002, 61, 247.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 39
    • 0034948696 scopus 로고    scopus 로고
    • Erratum
    • Ballesteros, J. A.; Shi, L.; Javitch, J. A. Structural Mimicry in G Protein-Coupled Receptors: Implications of the High-Resolution Structure of Rhodopsin for Structure-Function Analysis of Rhodopsin-like Receptors. Mol. Pharmacol. 2001, 60, 1-19. Review. Erratum in: Mol. Pharmacol. 2002, 61, 247.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 247
  • 42
    • 0026458378 scopus 로고
    • Amino acid substitution matrixes from protein blocks
    • Henikoff, S.; Henikoff, J. G. Amino Acid Substitution Matrixes from Protein Blocks. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 10915-10919.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10915-10919
    • Henikoff, S.1    Henikoff, J.G.2
  • 43
    • 0003437299 scopus 로고    scopus 로고
    • July, Joseph Felsenstein, Department of Genome Sciences, University of Washington, Seattle, WA
    • PHYLIP Phylogeny Inference Package, Version 3.6, July 2002, Joseph Felsenstein, Department of Genome Sciences, University of Washington, Seattle, WA.
    • (2002) PHYLIP Phylogeny Inference Package, Version 3.6
  • 44
    • 6044242515 scopus 로고    scopus 로고
    • Graphics Application Lab., Department of Computer Science, Pusan National University, Pusan, South Korea
    • PhyloDraw, Version 0.8, Graphics Application Lab., Department of Computer Science, Pusan National University, Pusan, South Korea.
    • PhyloDraw, Version 0.8
  • 45
    • 0033026514 scopus 로고    scopus 로고
    • Improved performance in protein secondary structure prediction by inhomogeneous score combination
    • Guermeur, Y.; Geourjon, C.; Gallinari, P.; Deleage, G. Improved Performance in Protein Secondary Structure Prediction by Inhomogeneous Score Combination. Bioinformatics 1999, 15, 413-421.
    • (1999) Bioinformatics , vol.15 , pp. 413-421
    • Guermeur, Y.1    Geourjon, C.2    Gallinari, P.3    Deleage, G.4
  • 46
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Gamier, J.; Gibrat, J. F.; Robson, B. GOR Method for Predicting Protein Secondary Structure from Amino Acid Sequence. Methods Enzymol. 1996, 266, 540-553.
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Gamier, J.1    Gibrat, J.F.2    Robson, B.3
  • 47
    • 0023050277 scopus 로고
    • An algorithm for secondary structure determination in proteins based on sequence similarity
    • Levin, J. M.; Robson, B.; Gamier, J. An Algorithm for Secondary Structure Determination in Proteins Based on Sequence Similarity. FEBS Lett. 1986, 205, 303-308.
    • (1986) FEBS Lett. , vol.205 , pp. 303-308
    • Levin, J.M.1    Robson, B.2    Gamier, J.3
  • 48
    • 0029595442 scopus 로고
    • SOPMA: Significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
    • Geourjon, C.; Deleage, G. SOPMA: Significant Improvements in Protein Secondary Structure Prediction by Consensus Prediction from Multiple Alignments. Comput. Appl. Biosci. 1995, 11, 681-684.
    • (1995) Comput. Appl. Biosci. , vol.11 , pp. 681-684
    • Geourjon, C.1    Deleage, G.2
  • 52
    • 84986527718 scopus 로고
    • Derivation of class II force fields. 1. Methodology and quantum force field for the alkyl functional group and alkane molecules
    • Maple, J. R.; Hwang, M. J.; Stockfisch, T. P.; Dinur, U.; Waldman, M.; Ewig, C. S.; Hagler, A. T. Derivation of Class II Force Fields. 1. Methodology and Quantum Force Field for the Alkyl Functional Group and Alkane Molecules. J. Comput. Chem. 1994, 15, 162-182.
    • (1994) J. Comput. Chem. , vol.15 , pp. 162-182
    • Maple, J.R.1    Hwang, M.J.2    Stockfisch, T.P.3    Dinur, U.4    Waldman, M.5    Ewig, C.S.6    Hagler, A.T.7
  • 53
    • 0001345932 scopus 로고
    • Derivation of class II force fields. 2. Derivation and characterization of a class II force field, CFF93, for the alkyl functional group and alkane molecules
    • Hwang, M. J.; Stockfisch, T. P.; Hagler, A. T. Derivation of Class II Force Fields. 2. Derivation and Characterization of a Class II Force Field, CFF93, for the Alkyl Functional Group and Alkane Molecules. J. Am. Chem. Soc. 1994, 116, 2515-2525.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 2515-2525
    • Hwang, M.J.1    Stockfisch, T.P.2    Hagler, A.T.3
  • 55
    • 0037588974 scopus 로고    scopus 로고
    • 12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cysl1 and Cys270
    • 12 receptor by thiol reagents requires interaction with both extracellular cysteine residues, Cysl1 and Cys270. Blood 2003, 101, 3908-3914.
    • (2003) Blood , vol.101 , pp. 3908-3914
    • Ding, Z.1    Kim, S.2    Dorsam, R.T.3    Jin, J.4    Kunapuli, S.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.