메뉴 건너뛰기




Volumn 43, Issue 5, 2003, Pages 1520-1531

Molecular Dynamics Simulations of the Ligand-Induced Chemical Information Transfer in the 5-HT1A Receptor

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COMPUTER SIMULATION; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; PROTEINS;

EID: 0141890725     PISSN: 00952338     EISSN: None     Source Type: Journal    
DOI: 10.1021/ci034069c     Document Type: Article
Times cited : (33)

References (48)
  • 1
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • and references therein
    • Gether, U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr. Rev. 2000, 21, 90-113, and references therein.
    • (2000) Endocr. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 2
    • 0031897256 scopus 로고    scopus 로고
    • Constitutively Signaling G-protein coupled receptor and human disease
    • and references therein
    • Arvanitakis, L.; Geras-Raaka, E.; Gershengorn, M. C. Constitutively Signaling G-protein coupled receptor and human disease. Trends Endocrinol Metab. 1998, 9, 27-31, and references therein.
    • (1998) Trends Endocrinol Metab. , vol.9 , pp. 27-31
    • Arvanitakis, L.1    Geras-Raaka, E.2    Gershengorn, M.C.3
  • 3
    • 0029923235 scopus 로고    scopus 로고
    • How G proteins work: A continuing story
    • and references therein
    • Coleman, D. E.; Sprang, S. How G proteins work: a continuing story. TIBS 1996, 21, 41-44, and references therein.
    • (1996) TIBS , vol.21 , pp. 41-44
    • Coleman, D.E.1    Sprang, S.2
  • 7
    • 0030614337 scopus 로고    scopus 로고
    • The activation process of the ctis-adrenergic receptor: Potential role of protonation and hydrophobicity of a highly conserved aspartate
    • Scheer, A.; Fanelli, F.; Costa, T.; De Benedetti, P. G.; Cotecchia, S. The activation process of the ctis-adrenergic receptor: potential role of protonation and hydrophobicity of a highly conserved aspartate. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 808-813.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 808-813
    • Scheer, A.1    Fanelli, F.2    Costa, T.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 8
    • 0031712825 scopus 로고    scopus 로고
    • Ab initia modeling and molecular dynamics simulation of the α1b-adrenergic receptor activation
    • and references therein
    • Fanelli, P.; Menziani, M. C.; Scheer, A.; Cotecchia, S.; De Benedetti, P. G. Ab initia modeling and molecular dynamics simulation of the α1b-adrenergic receptor activation. Methods Companion Methods Emymol. 1998 14, 302-317, and references therein.
    • (1998) Methods Companion Methods Emymol. , vol.14 , pp. 302-317
    • Fanelli, P.1    Menziani, M.C.2    Scheer, A.3    Cotecchia, S.4    De Benedetti, P.G.5
  • 10
    • 0002047990 scopus 로고    scopus 로고
    • Theoretical study on receptor/G protein recognition: New insights into the mechanism of the au,-adrenergic receptor activation
    • Fanelli, F.; Menziani, M. C.; Scheer, A.; Cotecchia, S.; De Benedetti, P. G. Theoretical study on receptor/G protein recognition: new insights into the mechanism of the au,-adrenergic receptor activation. Int. J. Quantum Chem. 1999, 73, 71-83.
    • (1999) Int. J. Quantum Chem. , vol.73 , pp. 71-83
    • Fanelli, F.1    Menziani, M.C.2    Scheer, A.3    Cotecchia, S.4    De Benedetti, P.G.5
  • 11
    • 0033033914 scopus 로고    scopus 로고
    • Activation Mechanism of Human Oxytocin Receptor: A Combined Study of Experimental and Computer-Simulated Mutagenesis
    • Fanelli, F.; Barbier, P.; Zanchetta, D.; De Benedetti, P. G.; Chini, B. Activation Mechanism of Human Oxytocin Receptor: A Combined Study of Experimental and Computer-Simulated Mutagenesis. Mol. Pharmacol. 1999, 50, 214-225.
    • (1999) Mol. Pharmacol. , vol.50 , pp. 214-225
    • Fanelli, F.1    Barbier, P.2    Zanchetta, D.3    De Benedetti, P.G.4    Chini, B.5
  • 12
    • 0034628894 scopus 로고    scopus 로고
    • Theoretical study on mutation-induced activation of the luteinizing hormone receptor
    • Fanelli, F. Theoretical study on mutation-induced activation of the luteinizing hormone receptor. J. Mol. Biol. 2000, 296, 1333-1351.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1333-1351
    • Fanelli, F.1
  • 13
    • 0035824582 scopus 로고    scopus 로고
    • Mutational and computational analysis of the α1b-adrenergic receptor: Involvement of basic and hydrophobic residues in receptor activation and G protein coupling
    • Greasley, P. J.; Fanelli, F.; Scheer, A.; Abuin, L.; Nenniger-Tosato, M. ; De Benedetti, P. G.; Cotecchia. S. Mutational and computational analysis of the α1b-adrenergic receptor: involvement of basic and hydrophobic residues in receptor activation and G protein coupling. J. Biol Chem. 2001, 276, 46485-46494.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46485-46494
    • Greasley, P.J.1    Fanelli, F.2    Scheer, A.3    Abuin, L.4    Nenniger-Tosato, M.5    De Benedetti, P.G.6    Cotecchia, S.7
  • 15
    • 0037199930 scopus 로고    scopus 로고
    • Engineered and Simulated Mutations in Transmembrane Helices 6 and 7 of the Lutropin Receptor: A Model for Constitutive and Ligand-mediated Receptor Activation
    • Angelova, K.; Fanelli, F.; Puett, D. Engineered and Simulated Mutations in Transmembrane Helices 6 and 7 of the Lutropin Receptor: A Model for Constitutive and Ligand-mediated Receptor Activation. J. Biol. Chem, 2002, 277, 32202-32213.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32202-32213
    • Angelova, K.1    Fanelli, F.2    Puett, D.3
  • 23
    • 0000276092 scopus 로고    scopus 로고
    • 1 receptor ligands: Update 1997
    • and references therein
    • 1 receptor ligands: update 1997. Current Drugs 1997, 2, 351-372, and references therein.
    • (1997) Current Drugs , vol.2 , pp. 351-372
    • Glennon, R.A.1    Dukat, M.2
  • 24
    • 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
  • 25
    • 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
  • 27
    • 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
  • 28
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C.; Lesk, A. M. The relation between the divergence of sequence and structure in proteins. Embo J. 1986, 5, 823-826.
    • (1986) Embo J. , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 30
    • 0027996410 scopus 로고
    • Molecular Biology of serotonin (5-HT) receptors
    • and references therein
    • Peroutka, S. J. Molecular Biology of serotonin (5-HT) receptors. Synapse 1994, 18, 241-260, and references therein.
    • (1994) Synapse , vol.18 , pp. 241-260
    • Peroutka, S.J.1
  • 34
    • 0033522643 scopus 로고    scopus 로고
    • 1b-adrenergic receptor is a key switch residue involved in activation and catecholmine ring aromatic bonding
    • 1b-adrenergic receptor is a key switch residue involved in activation and catecholmine ring aromatic bonding. J. Biol. Chem. 1999, 274, 16320-16330.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16320-16330
    • Chen, S.1    Xu, M.2    Lin, F.3    Lee, D.4    Riek, P.5    Graham, R.M.6
  • 35
    • 0030577241 scopus 로고    scopus 로고
    • 1B-adrenergic receptor involved in agonist binding: Further differences in docking catecholamines to receptor subtypes
    • 1B-adrenergic receptor involved in agonist binding: further differences in docking catecholamines to receptor subtypes. FEBS Lett. 1996, 399, 9-13.
    • (1996) FEBS Lett. , vol.399 , pp. 9-13
    • Cavalli, A.1    Fanelli, F.2    Taddei, C.3    De Benedetti, P.G.4    Cotecchia, S.5
  • 36
    • 0037197848 scopus 로고    scopus 로고
    • Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography
    • Okada, T.; Fujiyoshi, Y.; Silow, M.; Navarro, J.; Landau, E. M.; Shichida, Y. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. PNAS 2002, 99, 5982-5987.
    • (2002) PNAS , vol.99 , pp. 5982-5987
    • Okada, T.1    Fujiyoshi, Y.2    Silow, M.3    Navarro, J.4    Landau, E.M.5    Shichida, Y.6
  • 38
    • 0028061193 scopus 로고
    • A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin
    • Amis, S.; Fahmy, K.; Hofmann, K. P.; Sakmar, T. P. A conserved carboxylic acid group mediates light-dependent proton uptake and signaling by rhodopsin. J. Biol. Chem. 1994, 269, 23879-23881.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23879-23881
    • Amis, S.1    Fahmy, K.2    Hofmann, K.P.3    Sakmar, T.P.4
  • 39
    • 0031446595 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state
    • Kim, J. M.; Altenbach, C.; Thurmond, R. L.; Khorana, H. G.; Hubbell, W. L. Structure and function in rhodopsin: rhodopsin mutants with a neutral amino acid at E134 have a partially activated conformation in the dark state. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 14273-14278.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 14273-14278
    • Kim, J.M.1    Altenbach, C.2    Thurmond, R.L.3    Khorana, H.G.4    Hubbell, W.L.5
  • 40
    • 0142004009 scopus 로고    scopus 로고
    • Strader, C., Sibley, D., Eds.; Wiley-Liss Pub.: New York; Structure/function analysis of GPCRs; Wess, J., Ed., and references therein
    • Cotecchia, S.; Fanelli, F.; Scheer, A.; De Benedetti, P. G. In Receptor Biochemistry and Methodology; Strader, C., Sibley, D., Eds.; Wiley-Liss Pub.: New York, 1999; Vol. III (Structure/function analysis of GPCRs; Wess, J., Ed.), pp 167-183, and references therein.
    • (1999) Receptor Biochemistry and Methodology , vol.3 , pp. 167-183
    • Cotecchia, S.1    Fanelli, F.2    Scheer, A.3    De Benedetti, P.G.4
  • 41
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6
    • Ballesteros, J. A.; Jensen, A. D.; Liapakis, G.; Rasmussen, S. G.; Shi, L.; Gether, U.; Javitch. J. A. Activation of the β2-adrenergic receptor involves disruption of an ionic lock between the cytoplasmic ends of transmembrane segments 3 and 6. J. Biol. Chem. 2001, 276, 29171-29177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1    Jensen, A.D.2    Liapakis, G.3    Rasmussen, S.G.4    Shi, L.5    Gether, U.6    Javitch, J.A.7
  • 42
    • 0037192858 scopus 로고    scopus 로고
    • Evidence for a model of agonist induced activation of 5Hydroxytryptamine2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6
    • Shapiro, D. A.; Kristiansen, K.; Weiner, D. M.; Kroeze, W. K.; Roth, B. L. J. Evidence for a model of agonist induced activation of 5Hydroxytryptamine2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6. J. Biol. Chem. 2002, 277, 11441-11449.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11441-11449
    • Shapiro, D.A.1    Kristiansen, K.2    Weiner, D.M.3    Kroeze, W.K.4    Roth, B.L.J.5
  • 44
    • 0035856560 scopus 로고    scopus 로고
    • Functional Role of a Conserved Motif in TM6 of the Rat μ Opioid Receptor: Constitutively Active and Inactive Receptors Result from Substitutions of Thr6.34(279) with Lys and Asp
    • Huang, P.; Li, J.; Chen, C.; Visiers, I.; Weinstein, H.; LiuChen, L.-J. Functional Role of a Conserved Motif in TM6 of the Rat μ Opioid Receptor: Constitutively Active and Inactive Receptors Result from Substitutions of Thr6.34(279) with Lys and Asp. Biochemistry 2001, 40, 13501-13509.
    • (2001) Biochemistry , vol.40 , pp. 13501-13509
    • Huang, P.1    Li, J.2    Chen, C.3    Visiers, I.4    Weinstein, H.5    LiuChen, L.-J.6
  • 45
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swilves and switches: The role of prolines in signaling via transmembrane α-helices
    • and references therein
    • Sansom, M. S. P.; Weinstein, H. Hinges, swilves and switches: the role of prolines in signaling via transmembrane α-helices. TiPS 2000, 21, 445-451, and references therein.
    • (2000) TiPS , vol.21 , pp. 445-451
    • Sansom, M.S.P.1    Weinstein, H.2
  • 48
    • 0035498937 scopus 로고    scopus 로고
    • Receptor activation: What does rhodopsin structure tell us?
    • and references therein
    • Meng, E. C.; Bourne, H. Receptor activation: what does rhodopsin structure tell us? Trends Pharmacol. Sci. 2001, 22, 587-593, and references therein.
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.