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Volumn 4, Issue 6, 2004, Pages 337-347

Purine receptors: GPCR structure and agonist design

Author keywords

[No Author keywords available]

Indexed keywords

2 CHLORO 6 N CYCLOPENTYLADENOSINE; 6 N CYCLOPENTYLADENOSINE; ADENOSINE A1 RECEPTOR AGONIST; ADENOSINE A2A RECEPTOR; ADENOSINE A3 RECEPTOR; ADENOSINE A3 RECEPTOR AGONIST; ADENOSINE A3 RECEPTOR ANTAGONIST; ADENOSINE RECEPTOR; ADENOSINE RECEPTOR BLOCKING AGENT; ADENOSINE RECEPTOR STIMULATING AGENT; G PROTEIN COUPLED RECEPTOR; MRS 1292; MRS 1898; MRS 2365; MRS 3558; PURINE P2Y RECEPTOR; PURINE P2Y1 RECEPTOR; PURINE RECEPTOR; PURINERGIC RECEPTOR BLOCKING AGENT; PURINERGIC RECEPTOR STIMULATING AGENT; RECEPTOR SUBTYPE; UNCLASSIFIED DRUG;

EID: 12344310323     PISSN: 15340384     EISSN: None     Source Type: Journal    
DOI: 10.1124/mi.4.6.7     Document Type: Review
Times cited : (12)

References (55)
  • 1
    • 0035117505 scopus 로고    scopus 로고
    • Minireview: Insights into G protein-coupled receptor function using molecular models
    • Gershengorn, M.C. and Osman, R. Minireview: Insights into G protein-coupled receptor function using molecular models. Endocrinology 142, 2-10 (2001).
    • (2001) Endocrinology , vol.142 , pp. 2-10
    • Gershengorn, M.C.1    Osman, R.2
  • 2
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers, I., Ballesteros, J.A., and Weinstein, H. Three-dimensional representations of G protein-coupled receptor structures and mechanisms. Methods Enzymol. 343, 329-371 (2002).
    • (2002) Methods Enzymol. , vol.343 , pp. 329-371
    • Visiers, I.1    Ballesteros, J.A.2    Weinstein, H.3
  • 3
    • 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
    • Ballesteros, J.A., Shi, L., and 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. 60, 1-19 (2001).
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 4
    • 0034604451 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: A G protein-coupled receptor
    • Palczewski, K. et al. Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289, 739-745 (2000).
    • (2000) Science , vol.289 , pp. 739-745
    • Palczewski, K.1
  • 5
    • 0035209620 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXV. Nomenclature and classification of adeonsine receptors
    • Fredholm, B.B., IJzerman, A.P., Jacobson, K.A., Klotz, K.N., and Linden, J. International Union of Pharmacology. XXV. Nomenclature and classification of adeonsine receptors. Pharmacol. Rev. 53, 527-552 (2001).
    • (2001) Pharmacol. Rev. , vol.53 , pp. 527-552
    • Fredholm, B.B.1    IJzerman, A.P.2    Jacobson, K.A.3    Klotz, K.N.4    Linden, J.5
  • 6
    • 0033756267 scopus 로고    scopus 로고
    • Molecular pharmacology of P2Y-receptors. Naunyn Schmiedebergs
    • von Kügelgen, I. and Wetter, A. Molecular pharmacology of P2Y-receptors. Naunyn Schmiedebergs Arch. Pharmacol. 362, 310-323 (2000).
    • (2000) Arch. Pharmacol. , vol.362 , pp. 310-323
    • von Kügelgen, I.1    Wetter, A.2
  • 7
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine: An endogenous regulator of innate immunity
    • Haskó, G. and Cronstein, B.N. Adenosine: An endogenous regulator of innate immunity. Trends Immunol. 25, 33-39 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 33-39
    • Haskó, G.1    Cronstein, B.N.2
  • 9
    • 0033624056 scopus 로고    scopus 로고
    • Ischemic preconditioning: From basic mechanisms to clinical applications
    • Nakano, A., Cohen, M.V., and Downey, J.M. Ischemic preconditioning: from basic mechanisms to clinical applications. Pharmacol. Ther. 86, 263-275 (2000).
    • (2000) Pharmacol. Ther. , vol.86 , pp. 263-275
    • Nakano, A.1    Cohen, M.V.2    Downey, J.M.3
  • 11
    • 0037030495 scopus 로고    scopus 로고
    • Evidence for involvement of Wnt signaling pathway in IB-MECA medicated suppression of melanoma cells
    • Fishman, P., Madi, L., Bar-Yehuda, S., Barer, F., Del Valle, L., and Khalili, K. Evidence for involvement of Wnt signaling pathway in IB-MECA medicated suppression of melanoma cells. Oncogene. 21 4060-4064 (2002).
    • (2002) Oncogene , vol.21 , pp. 4060-4064
    • Fishman, P.1    Madi, L.2    Bar-Yehuda, S.3    Barer, F.4    Del Valle, L.5    Khalili, K.6
  • 13
    • 0033760792 scopus 로고    scopus 로고
    • Adenosine receptor ligands - Recent developments
    • Müller, C.E. Adenosine receptor ligands - recent developments. Curr. Med. Chem. 7, 1269-1288 (2000).
    • (2000) Curr. Med. Chem. , vol.7 , pp. 1269-1288
    • Müller, C.E.1
  • 16
    • 10744227271 scopus 로고    scopus 로고
    • 3 adenosine receptors: Modification of the ribose moiety
    • 3 adenosine receptors: Modification of the ribose moiety. Biochem. Pharmacol. 67, 893-901 (2004).
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 893-901
    • Gao, Z.G.1    Jeong, L.S.2    Moon, H.R.3
  • 17
    • 2442507658 scopus 로고    scopus 로고
    • Modulation of adenosine receptor affinity and intrinsic efficacy in nucleosides substituted at the 2-position
    • Ohno, M., Gao, Z.G., van Rompaey, P. et al. Modulation of adenosine receptor affinity and intrinsic efficacy in nucleosides substituted at the 2-position. Bioorganic Med. Chem. 12, 2995-3007 (2004).
    • (2004) Bioorganic Med. Chem. , vol.12 , pp. 2995-3007
    • Ohno, M.1    Gao, Z.G.2    van Rompaey, P.3
  • 19
    • 5144219791 scopus 로고    scopus 로고
    • 2-Substituted adenosine derivatives: Affinity and efficacy at four subtypes of human adenosine receptors
    • Gao, Z.G., Mamedova, L., Chen, P., and Jacobson, K.A. 2-Substituted adenosine derivatives: Affinity and efficacy at four subtypes of human adenosine receptors. Biochem. Pharmacol. 68 1985-1993 (2004).
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1985-1993
    • Gao, Z.G.1    Mamedova, L.2    Chen, P.3    Jacobson, K.A.4
  • 20
    • 0016043729 scopus 로고
    • Sulphur-methylene isosterism in the development of metiamide, a new histamine H2-receptor antagonist
    • Black, J.W., Durant, G.J., Emmett, J.C., and Ganellin, C.R. Sulphur-methylene isosterism in the development of metiamide, a new histamine H2-receptor antagonist. Nature 248, 65-67 (1974).
    • (1974) Nature , vol.248 , pp. 65-67
    • Black, J.W.1    Durant, G.J.2    Emmett, J.C.3    Ganellin, C.R.4
  • 23
    • 0037380778 scopus 로고    scopus 로고
    • Knock-out mice reveal tissue-specific roles of P2Y receptor subtypes in different epithelia
    • Dubyak, G.R. Knock-out mice reveal tissue-specific roles of P2Y receptor subtypes in different epithelia. Mol. Pharmacol. 63 773-776 (2003).
    • (2003) Mol. Pharmacol. , vol.63 , pp. 773-776
    • Dubyak, G.R.1
  • 24
    • 2442427376 scopus 로고    scopus 로고
    • Metabolism of P2 receptor agonists in human airways: Implications for mucociliary clearance and cystic fibrosis
    • Picher, M., Burch, L.H., and Boucher, R.C. Metabolism of P2 receptor agonists in human airways: Implications for mucociliary clearance and cystic fibrosis. J. Biol. Chem. 279, 20234-20241 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 20234-20241
    • Picher, M.1    Burch, L.H.2    Boucher, R.C.3
  • 25
    • 1542601104 scopus 로고    scopus 로고
    • Differential involvement of the P2Y1 and P2Y12 receptors in platelet procoagulant activity
    • Leon, C., Ravanat, C., Freund, M., Cazenave, J.P., and Gachet, C. Differential involvement of the P2Y1 and P2Y12 receptors in platelet procoagulant activity. Arterioscler. Thromb. Vasc. Biol. 23, 1941-1947 (2003).
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , pp. 1941-1947
    • Leon, C.1    Ravanat, C.2    Freund, M.3    Cazenave, J.P.4    Gachet, C.5
  • 28
    • 0141992805 scopus 로고    scopus 로고
    • Three-dimensional models for beta-adrenergic receptor complexes with agonists and antagonists
    • Furse, K.E. and Lybrand, T.P. Three-dimensional models for beta-adrenergic receptor complexes with agonists and antagonists. J. Med. Chem. 46, 4450-4462(2003).
    • (2003) J. Med. Chem. , vol.46 , pp. 4450-4462
    • Furse, K.E.1    Lybrand, T.P.2
  • 29
    • 4444274752 scopus 로고    scopus 로고
    • PREDICT modeling and in-silico screening for G protein-coupled receptors
    • Shacham, S., Marantz, Y., Bar-Haim, S. et al. PREDICT modeling and in-silico screening for G protein-coupled receptors. Proteins. 57, 51-86 (2004).
    • (2004) Proteins , vol.57 , pp. 51-86
    • Shacham, S.1    Marantz, Y.2    Bar-Haim, S.3
  • 30
    • 0242267908 scopus 로고    scopus 로고
    • 2-Substitution of adenine nucleotide analogues containing a bicyclo[3.1.0]hexane ring system locked in a Northern conformation: Enhanced potency as P2Y1 receptor antagonists
    • Kim, H.S., Ohno, M., Xu, B. et al. 2-Substitution of adenine nucleotide analogues containing a bicyclo[3.1.0]hexane ring system locked in a Northern conformation: Enhanced potency as P2Y1 receptor antagonists. J. Med. Chem. 46, 4974-4987 (2003).
    • (2003) J. Med. Chem. , vol.46 , pp. 4974-4987
    • Kim, H.S.1    Ohno, M.2    Xu, B.3
  • 33
    • 6044234752 scopus 로고    scopus 로고
    • Architecture of P2Y nucleotide receptors: Structural comparison based on sequence analysis, mutagenesis, and homology modeling
    • Costanzi, S., Mamedova, L., Gao, Z.G., and Jacobson, K.A. Architecture of P2Y nucleotide receptors: Structural comparison based on sequence analysis, mutagenesis, and homology modeling. J. Med. Chem. 47, 5393-5404 (2004).
    • (2004) J. Med. Chem. , vol.47 , pp. 5393-5404
    • Costanzi, S.1    Mamedova, L.2    Gao, Z.G.3    Jacobson, K.A.4
  • 35
    • 0035935737 scopus 로고    scopus 로고
    • Neoceptor concept based on molecular complementarity in GPCRs: A mutant adenosine A3 receptor with selectively enhanced affinity for amine-modified nucleosides
    • Jacobson, K.A., Gao, Z.G., Chen, A. et al. Neoceptor concept based on molecular complementarity in GPCRs: A mutant adenosine A3 receptor with selectively enhanced affinity for amine-modified nucleosides J. Med. Chem. 44, 4125-4136 (2001).
    • (2001) J. Med. Chem. , vol.44 , pp. 4125-4136
    • Jacobson, K.A.1    Gao, Z.G.2    Chen, A.3
  • 36
    • 0037179640 scopus 로고    scopus 로고
    • Structural determinants of A3 adenosine receptor activation: Nucleoside ligands at the agonist/antagonist boundary
    • Gao, Z.G., Kim, S.K., Biadatti, T., Chen, W., Lee, K., Barak, D., Kim, S.G., Johnson, C.R., and Jacobson, K.A. Structural determinants of A3 adenosine receptor activation: Nucleoside ligands at the agonist/antagonist boundary. J. Med. Chem. 45, 4471-4484 (2002).
    • (2002) J. Med. Chem. , vol.45 , pp. 4471-4484
    • Gao, Z.G.1    Kim, S.K.2    Biadatti, T.3    Chen, W.4    Lee, K.5    Barak, D.6    Kim, S.G.7    Johnson, C.R.8    Jacobson, K.A.9
  • 37
    • 0015511563 scopus 로고
    • Conformational analysis of the sugar ring in nucleosides and nucleotides. A new description using the concept of pseudorotation
    • Altona, C., and Sundaralingham, M. Conformational analysis of the sugar ring in nucleosides and nucleotides. A new description using the concept of pseudorotation. J. Am. Chem. Soc. 94, 8205 (1972).
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 8205
    • Altona, C.1    Sundaralingham, M.2
  • 38
    • 0029815436 scopus 로고    scopus 로고
    • Nucleosides with a twist. Can fixed forms of sugar ring pucker influence biological activity in nucleosides and oligonucleotides?
    • Marquez, V.E., Siddiqui, M.A., Ezzitouni, A., Russ, P., Wang, J., Wagner, R.W., and Matteucci, M.D. Nucleosides with a twist. Can fixed forms of sugar ring pucker influence biological activity in nucleosides and oligonucleotides? J. Med. Chem. 39, 3739-3747 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 3739-3747
    • Marquez, V.E.1    Siddiqui, M.A.2    Ezzitouni, A.3    Russ, P.4    Wang, J.5    Wagner, R.W.6    Matteucci, M.D.7
  • 42
    • 0028171408 scopus 로고
    • A1 adenosine receptors. Two amino acids are responsible for species differences in ligand recognition
    • Tucker, A.L., Robeva, A.S., Taylor, H.E., Holeton, D., Bockner, M., Lynch, K.R., and Linden, J. A1 adenosine receptors. Two amino acids are responsible for species differences in ligand recognition. J. Biol. Chem. 269, 27900-27906 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 27900-27906
    • Tucker, A.L.1    Robeva, A.S.2    Taylor, H.E.3    Holeton, D.4    Bockner, M.5    Lynch, K.R.6    Linden, J.7
  • 43
    • 0033524916 scopus 로고    scopus 로고
    • Identification of the adenine binding site of the human A1 adenosine receptor
    • Rivkees, S.A., Barbhaiya, H., and IJzerman, A. Identification of the adenine binding site of the human A1 adenosine receptor. J. Biol. Chem. 274, 3617-3621 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3617-3621
    • Rivkees, S.A.1    Barbhaiya, H.2    IJzerman, A.3
  • 44
    • 0035932989 scopus 로고    scopus 로고
    • Agonist-induced conformational changes in the G protein-coupling domain of the beta 2 adrenergic receptor
    • Ghanouni, P., Steenhuis, J.J., Farrens, D.L., and Kobilka, B.K. Agonist-induced conformational changes in the G protein-coupling domain of the beta 2 adrenergic receptor. Proc. Natl. Acad. Sci. U.S.A. 98, 5997-6002 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5997-6002
    • Ghanouni, P.1    Steenhuis, J.J.2    Farrens, D.L.3    Kobilka, B.K.4
  • 45
    • 11144225093 scopus 로고    scopus 로고
    • Common structural basis for constitutive activity of the ghrelin receptor family
    • 10.1074/jbc.M40767200
    • Hoist, B., Holliday, N.D., Bach, A., Elling, C.E., Cox, H.M., and Schwartz, T.W. Common structural basis for constitutive activity of the ghrelin receptor family. J. Biol. Chem. 10.1074/jbc.M40767200.
    • J. Biol. Chem.
    • Hoist, B.1    Holliday, N.D.2    Bach, A.3    Elling, C.E.4    Cox, H.M.5    Schwartz, T.W.6
  • 46
    • 12344300378 scopus 로고    scopus 로고
    • 3 adenosine-receptor antagonist MRS 1292 inhibits adenosine-triggered human nonpigmented ciliary epithelial cell fluid release and reduces mouse intraocular pressure
    • (unpublished results)
    • 3 adenosine-receptor antagonist MRS 1292 inhibits adenosine-triggered human nonpigmented ciliary epithelial cell fluid release and reduces mouse intraocular pressure (unpublished results).
    • Yang, H.1    Avila, M.Y.2    Peterson-Yantorno, K.3    Coca-Prados, M.4    Stone, R.A.5    Jacobson, K.A.6    Civan, M.M.7
  • 50
    • 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. 41, 1456-1466 (1998).
    • (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


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