메뉴 건너뛰기




Volumn 1, Issue 2, 2005, Pages 98-103

Linking agonist binding to histamine H1 receptor activation

Author keywords

[No Author keywords available]

Indexed keywords

HISTAMINE AGONIST; HISTAMINE H1 RECEPTOR; SERINE;

EID: 26444467486     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio714     Document Type: Article
Times cited : (89)

References (47)
  • 2
    • 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
  • 3
    • 34447252350 scopus 로고    scopus 로고
    • Conformational plasticity of GPCR binding sites; structural basis for evolutionary diversity in ligand recognition
    • (ed. Devi, L.A.) (Humana Press, Totowa
    • Deupi, X. et al. Conformational plasticity of GPCR binding sites; structural basis for evolutionary diversity in ligand recognition. in The G Protein-Coupled Receptors Handbook (ed. Devi, L.A.) (Humana Press, Totowa, 2005).
    • (2005) The G Protein-Coupled Receptors Handbook
    • Deupi, X.1
  • 4
    • 0037452868 scopus 로고    scopus 로고
    • Sequence analyses of G-protein-coupled receptors: Similarities to rhodopsin
    • Mirzadegan, T., Benko, G., Filipek, S. & Palczewski, K. Sequence analyses of G-protein-coupled receptors: similarities to rhodopsin. Biochemistry 42, 2759-2767 (2003).
    • (2003) Biochemistry , vol.42 , pp. 2759-2767
    • Mirzadegan, T.1    Benko, G.2    Filipek, S.3    Palczewski, K.4
  • 5
    • 0036169280 scopus 로고    scopus 로고
    • The binding site of aminergic G protein-coupled receptors: The transmembrane segments and second extracellular loop
    • Shi, L. & Javitch, J.A. The binding site of aminergic G protein-coupled receptors: the transmembrane segments and second extracellular loop. Annu. Rev. Pharmacol. Toxicol. 42, 437-467 (2002).
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 437-467
    • Shi, L.1    Javitch, J.A.2
  • 6
    • 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. 25, 366-428 (1995).
    • (1995) Methods Neurosci , vol.25 , pp. 366-428
    • Ballesteros, J.A.1    Weinstein, H.2
  • 9
    • 1642369857 scopus 로고    scopus 로고
    • 1-receptorbindingpocketof histaprodifens
    • 1-receptorbindingpocketof histaprodifens. Eur. J. Pharmacol. 487, 55-63 (2004).
    • (2004) Eur. J. Pharmacol. , vol.487 , pp. 55-63
    • Bruysters, M.1
  • 11
    • 0033569709 scopus 로고    scopus 로고
    • 1 receptor
    • 1 receptor. J. Biol. Chem. 274, 29994-30000 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 29994-30000
    • Wieland, K.1
  • 15
  • 16
    • 0034787251 scopus 로고    scopus 로고
    • Three-dimensional representations of G protein-coupled receptor structures and mechanisms
    • Visiers, I., Ballesteros, J.A. & 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
  • 17
    • 0037174606 scopus 로고    scopus 로고
    • 2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • 2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch. J. Biol. Chem. 277, 40989-40996 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 40989-40996
    • Shi, L.1
  • 18
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • Ruprecht, J.J., Mielke, T., Vogel, R., Villa, C. & Schertler, G.F.X. Electron crystallography reveals the structure of metarhodopsin I. EMBO J. 23, 3609-3620 (2004).
    • (2004) EMBO J , vol.23 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 19
    • 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. et al. 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. 276, 29171-29177 (2001).
    • (2001) J. Biol. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1
  • 20
    • 0037066181 scopus 로고    scopus 로고
    • 2A receptor by disruption of the ionic lock of the arginine cage
    • 2A receptor by disruption of the ionic lock of the arginine cage. Int. J. Quantum Chem. 88, 65-75 (2002).
    • (2002) Int. J. Quantumchem. , vol.88 , pp. 65-75
    • Visiers, I.1
  • 22
    • 0028276459 scopus 로고
    • A model for G protein interaction in G protein coupled receptors
    • Oliveira, L., Paiva, A.C.M., Sander, C. & Vriend, G. A model for G protein interaction in G protein coupled receptors. Trends Pharmacol. Sci. 15, 170-172 (1994).
    • (1994) Trends Pharmacol. Sci. , vol.15 , pp. 170-172
    • Oliveira, L.1    Paiva, A.C.M.2    Sander, C.3    Vriend, G.4
  • 23
    • 0034603147 scopus 로고    scopus 로고
    • 2 adrenoceptor function. Evidence forprotonation-dependentactivation
    • 2 adrenoceptor function. Evidence for protonation-dependentactivation. J. Biol. Chem. 275, 3121-3127 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 3121-3127
    • Ghanouni, P.1
  • 24
    • 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 274, 768-770 (1996).
    • (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
  • 26
    • 0035498937 scopus 로고    scopus 로고
    • Receptoractivation: Whatdoestherhodopsin structuretell us?
    • Meng, E.C. & Bourne, H.R. Receptoractivation: whatdoestherhodopsin structuretell us? Trends Pharmacol. Sci. 22, 587-593 (2001).
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 587-593
    • Meng, E.C.1    Bourne, H.R.2
  • 27
    • 0035933839 scopus 로고    scopus 로고
    • A conserved Asn in transmembrane helix 7 is an on/off switch inthe activation of the thyrotropin receptor
    • Govaerts, C. et al. A conserved Asn in transmembrane helix 7 is an on/off switch in the activation of the thyrotropin receptor. J. Biol. Chem. 276, 22991-22999 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22991-22999
    • Govaerts, C.1
  • 28
    • 20444478293 scopus 로고    scopus 로고
    • An activation switch in the rhodopsin family of G protein coupledreceptors: The thyrotropin receptor
    • Urizar, E. et al. An activation switch in the rhodopsin family of G protein coupled receptors: the thyrotropin receptor. J. Biol. Chem. 280, 17135-17141 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 17135-17141
    • Urizar, E.1
  • 29
    • 0037165664 scopus 로고    scopus 로고
    • A conserved Asn in TM7 of the thyrotropin receptor is a common requirementfor activation byboth mutations and itsnatural agonist
    • Claeysen, S. et al. A conserved Asn in TM7 of the thyrotropin receptor is a common requirementfor activation byboth mutations and itsnatural agonist. FEBSLett. 517, 195-200 (2002).
    • (2002) Febslett , vol.517 , pp. 195-200
    • Claeysen, S.1
  • 30
    • 0037285444 scopus 로고    scopus 로고
    • Rhodopsin structure, dynamics, and activation: A perspective from crystallography, site-directed spin label-ing, sulfhydryl reactivity, and disulfide cross-linking
    • Hubbell, W.L., Altenbach, C., Hubbell, C.M. & Khorana, H.G. Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin label-ing, sulfhydryl reactivity, and disulfide cross-linking. Adv. Protein Chem. 63, 243-290 (2003).
    • (2003) Adv. Protein Chem. , vol.63 , pp. 243-290
    • Hubbell, W.L.1    Altenbach, C.2    Hubbell, C.M.3    Khorana, H.G.4
  • 31
    • 0029886215 scopus 로고    scopus 로고
    • 2A receptor. Ser3.36(159) provides a second interaction site for the protonated amine of serotonin but not of lysergic acid diethylamide or bufotenin
    • 2A receptor. Ser3.36(159) provides a second interaction site for the protonated amine of serotonin but not of lysergic acid diethylamide or bufotenin. J. Biol. Chem. 271, 14672-14675 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 14672-14675
    • Almaula, N.1    Ebersole, B.J.2    Zhang, D.3    Weinstein, H.4    Sealfon, S.C.5
  • 32
    • 0026485739 scopus 로고
    • Acetylcholine receptor channelstructure probed in cysteine-substitution mutants
    • Akabas, M.H., Stauffer, D.A., Xu, M. & Karlin, A. Acetylcholine receptor channel structure probed in cysteine-substitution mutants. Science 258, 307-310 (1992).
    • (1992) Science , vol.258 , pp. 307-310
    • Akabas, M.H.1    Stauffer, D.A.2    Xu, M.3    Karlin, A.4
  • 33
    • 0034752736 scopus 로고    scopus 로고
    • 1-receptor activation of nuclear factor-κB: Roles for Gβγ-and Gαq/11-subunits in constitutive and agonist-mediated signaling
    • 1-receptor activation of nuclear factor-κB: roles for Gβγ-and Gαq/11-subunits in constitutive and agonist-mediated signaling. Mol. Pharmacol. 60, 1133-1142 (2001).
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1133-1142
    • Bakker, R.A.1    Schoonus, S.B.2    Smit, M.J.3    Timmerman, H.4    Leurs, R.5
  • 34
    • 0033747337 scopus 로고    scopus 로고
    • Serineand threonine residues bend α-helices in the χ1 = g- conformation
    • Ballesteros, J.A., Deupi, X., Olivella, M., Haaksma, E.E.J. & Pardo, L. Serine and threonine residues bend α-helices in the χ1 = g- conformation. Biophys. J. 79, 2754-2760 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 2754-2760
    • Ballesteros, J.A.1    Deupi, X.2    Olivella, M.3    Haaksma, E.E.J.4    Pardo, L.5
  • 35
    • 9144224914 scopus 로고    scopus 로고
    • 1 receptor activation
    • 1 receptor activation. J. Biol. Chem. 279, 48024-48037 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 48024-48037
    • McAllister, S.D.1
  • 37
    • 0029773758 scopus 로고    scopus 로고
    • Modifications of vectors pEF-BOS, pcDNA1 and pcDNA3 result in improved convenience and expression
    • Goldman, L.A., Cutrone, E.C., Kotenko, S.V., Krause, C.D. & Langer, J.A. Modifications of vectors pEF-BOS, pcDNA1 and pcDNA3 result in improved convenience and expression. Biotechniques 21, 1013-1015 (1996).
    • (1996) Biotechniques , vol.21 , pp. 1013-1015
    • Goldman, L.A.1    Cutrone, E.C.2    Kotenko, S.V.3    Krause, C.D.4    Langer, J.A.5
  • 39
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 40
    • 0037197848 scopus 로고    scopus 로고
    • Functional role of internal water molecules in rhodopsin revealed byX-ray crystallography
    • Okada, T. et al. Functional role of internal water molecules in rhodopsin revealed by X-ray crystallography. Proc. Natl. Acad. Sci. USA 99, 5982-5987 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5982-5987
    • Okada, T.1
  • 41
    • 0036084957 scopus 로고    scopus 로고
    • 1a receptor ligands to explore the three-dimensional structure ofthe receptor
    • 1a receptor ligands to explore the three-dimensional structure of the receptor. Mol. Pharmacol. 62, 15-21 (2002).
    • (2002) Mol. Pharmacol. , vol.62 , pp. 15-21
    • López-Rodriguez, M.L.1
  • 43
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm forrapid protein side-chain prediction
    • Canutescu, A.A., Shelenkov, A.A. & Dunbrack, R.L., Jr. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12, 2001-2014 (2003).
    • (2003) Protein Sci , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack, R.L.3
  • 44
    • 84984774441 scopus 로고    scopus 로고
    • AMBER 8, UniversityofCalifornia, San Francisco
    • Case, D.A. et al. AMBER 8. (UniversityofCalifornia, San Francisco, 2004).
    • (2004)
    • Case, D.A.1
  • 45
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biologicalmolecules?
    • Wang, J., Cieplak, P. & Kollman, P.A. How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J. Comput. Chem. 21, 1049-1074 (2000).
    • (2000) J. Comput. Chem , vol.21 , pp. 1049-1074
    • Wang, J.1    Cieplak, P.2    Kollman, P.A.3
  • 46
    • 84870538517 scopus 로고    scopus 로고
    • Gaussian Inc., Pittsburgh Pennsylva-nia
    • Frisch, M.J. et al. Gaussian 98, Revision A.11. (Gaussian Inc., Pittsburgh Pennsylva-nia, 2001).
    • (2001) Gaussian 98
    • Frisch, M.J.1
  • 47
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots ofprotein structures
    • Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.