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Volumn 170, Issue 1, 2010, Pages 10-20

Predicted 3D structures for adenosine receptors bound to ligands: Comparison to the crystal structure

Author keywords

Adenosine; Docking; GPCRs; Ligand binding; Membrane protein structure; Modeling; Receptor; Structure prediction

Indexed keywords

4 [2 [7 AMINO 2 (2 FURYL) 1,2,4 TRIAZOLO[2,3 A][1,3,5]TRIAZIN 5 YLAMINO]ETHYL]PHENOL; ADENOSINE RECEPTOR; G PROTEIN COUPLED RECEPTOR;

EID: 77950519682     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.01.001     Document Type: Article
Times cited : (49)

References (35)
  • 1
    • 49649120129 scopus 로고    scopus 로고
    • The structure of human serotonin 2c G protein-coupled receptor bound to agonists and antagonists
    • Bray J.K., Goddard W.A. The structure of human serotonin 2c G protein-coupled receptor bound to agonists and antagonists. J. Mol. Graph. Model. 2008, 27:66-81.
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 66-81
    • Bray, J.K.1    Goddard, W.A.2
  • 3
    • 0001691450 scopus 로고    scopus 로고
    • Protein fold determination from sparse distance restraints: the restrained generic protein direct Monte Carlo method
    • Debe D., Carlson M.J., Sadanobu J., Chan S.I., Goddard W.A. Protein fold determination from sparse distance restraints: the restrained generic protein direct Monte Carlo method. J. Phys. Chem. B 1999, 103:3001-3008.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3001-3008
    • Debe, D.1    Carlson, M.J.2    Sadanobu, J.3    Chan, S.I.4    Goddard, W.A.5
  • 4
    • 0029907599 scopus 로고    scopus 로고
    • Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin
    • Farrens D.L., Altenbach C., Yang K., Hubbell W.L., Khorana H.G. Requirement of rigid-body motion of transmembrane helices for light activation of rhodopsin. Science 1996, 274:768-770.
    • (1996) Science , vol.274 , pp. 768-770
    • Farrens, D.L.1    Altenbach, C.2    Yang, K.3    Hubbell, W.L.4    Khorana, H.G.5
  • 7
    • 34548724959 scopus 로고    scopus 로고
    • Prediction of the 3D structure of FMRF-amide neuropeptides bound to the mouse MrgC11 GPCR and experimental validation
    • Heo J., Han S.K., Vaidehi N., Wendel J., Kekenes-Huskey P., Goddard W.A. Prediction of the 3D structure of FMRF-amide neuropeptides bound to the mouse MrgC11 GPCR and experimental validation. Chem. Biol. Chem. 2007, 8:1527-1539.
    • (2007) Chem. Biol. Chem. , vol.8 , pp. 1527-1539
    • Heo, J.1    Han, S.K.2    Vaidehi, N.3    Wendel, J.4    Kekenes-Huskey, P.5    Goddard, W.A.6
  • 11
    • 58149267930 scopus 로고    scopus 로고
    • Flat-bottom strategy for improved accuracy in protein side-chain placements
    • Kam V.W.T., Goddard W.A. Flat-bottom strategy for improved accuracy in protein side-chain placements. J. Chem. Theor. Comput. 2008, 4:2160-2169.
    • (2008) J. Chem. Theor. Comput. , vol.4 , pp. 2160-2169
    • Kam, V.W.T.1    Goddard, W.A.2
  • 12
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K., Toh H., Miyata T. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acid Res. 2005, 33:511-518.
    • (2005) Nucleic Acid Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 13
    • 2142823785 scopus 로고    scopus 로고
    • Agonist binding: a multistep process
    • Kobilka B. Agonist binding: a multistep process. Mol. Pharmacol. 2004, 65:1060-1062.
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1060-1062
    • Kobilka, B.1
  • 15
    • 33749615286 scopus 로고    scopus 로고
    • Continuous self-avoiding walk with application to the description of polymer chains
    • Li Y.Y., Goddard W.A. Continuous self-avoiding walk with application to the description of polymer chains. J. Phys. Chem. B 2006, 110:18134-18137.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 18134-18137
    • Li, Y.Y.1    Goddard, W.A.2
  • 17
    • 33749521608 scopus 로고    scopus 로고
    • Latest development in drug discovery on G protein-coupled receptors
    • Lundstrom K. Latest development in drug discovery on G protein-coupled receptors. Curr. Prot. Peptide Sci. 2006, 7:465-470.
    • (2006) Curr. Prot. Peptide Sci. , vol.7 , pp. 465-470
    • Lundstrom, K.1
  • 18
    • 9144240095 scopus 로고
    • DREIDING - a generic force-field for molecular simulations
    • Mayo S.L., Olafson B.D., Goddard W.A. DREIDING - a generic force-field for molecular simulations. J. Phys. Chem. 1990, 94:8897-8909.
    • (1990) J. Phys. Chem. , vol.94 , pp. 8897-8909
    • Mayo, S.L.1    Olafson, B.D.2    Goddard, W.A.3
  • 19
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: what does the rhodopsin structure tell us?
    • Meng E.C., Bourne H.R. Receptor activation: what does the rhodopsin structure tell us?. Trends Pharmacol. Sci. 2001, 22:587-593.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 23
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G-protein-coupled receptor opsin
    • U33
    • Park J.H., Scheerer P., Hofmann K.P., Choe H.W., Ernst O.P. Crystal structure of the ligand-free G-protein-coupled receptor opsin. Nature 2008, 454:183. U33.
    • (2008) Nature , vol.454 , pp. 183
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 24
    • 33748643600 scopus 로고    scopus 로고
    • The predicted 3D structures of the human M1 muscarinic acetylcholine receptor with agonist or antagonist bound
    • Peng J.Y.C., Vaidehi N., Hall S.E., Goddard W.A. The predicted 3D structures of the human M1 muscarinic acetylcholine receptor with agonist or antagonist bound. Chem. Med. Chem. 2006, 1:878-890.
    • (2006) Chem. Med. Chem. , vol.1 , pp. 878-890
    • Peng, J.Y.C.1    Vaidehi, N.2    Hall, S.E.3    Goddard, W.A.4
  • 26
    • 0035913537 scopus 로고    scopus 로고
    • Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions
    • Rocchia W., Alexov E., Honig B. Extending the applicability of the nonlinear Poisson-Boltzmann equation: multiple dielectric constants and multivalent ions. J. Phys. Chem. B 2001, 105:6507-6514.
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6507-6514
    • Rocchia, W.1    Alexov, E.2    Honig, B.3
  • 27
    • 0031123561 scopus 로고    scopus 로고
    • The continuous configurational Boltzmann biased direct Monte Carlo method for free energy properties of polymer chains
    • Sadanobu J., Goddard W.A. The continuous configurational Boltzmann biased direct Monte Carlo method for free energy properties of polymer chains. J. Chem. Phys. 1997, 106:6722-6729.
    • (1997) J. Chem. Phys. , vol.106 , pp. 6722-6729
    • Sadanobu, J.1    Goddard, W.A.2
  • 28
    • 28844478334 scopus 로고    scopus 로고
    • Genetic variation in G-protein-coupled receptors - consequences for G-protein-coupled receptors as drug targets
    • Tang C., Insel P. Genetic variation in G-protein-coupled receptors - consequences for G-protein-coupled receptors as drug targets. Expert Opin. Therap. Targets 2005, 9:1247-1265.
    • (2005) Expert Opin. Therap. Targets , vol.9 , pp. 1247-1265
    • Tang, C.1    Insel, P.2
  • 29
    • 1942487807 scopus 로고    scopus 로고
    • First principles predictions of the structure and function of G-protein-coupled receptors: validation for bovine rhodopsin
    • Trabanino R.J., Hall S.E., Vaidehi N., Floriano W.B., Kam V.W.T., Goddard W.A. First principles predictions of the structure and function of G-protein-coupled receptors: validation for bovine rhodopsin. Biophys. J. 2004, 86:1904-1921.
    • (2004) Biophys. J. , vol.86 , pp. 1904-1921
    • Trabanino, R.J.1    Hall, S.E.2    Vaidehi, N.3    Floriano, W.B.4    Kam, V.W.T.5    Goddard, W.A.6
  • 35
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley W.C., Creamer T.P., White S.H. Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides. Biochemistry 1996, 35:5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.