메뉴 건너뛰기




Volumn 2, Issue 8, 2006, Pages 417-422

Coupling ligand structure to specific conformational switches in the β2-adrenoceptor

Author keywords

[No Author keywords available]

Indexed keywords

3 ISOPROPYLAMINO 1 (7 METHYL 4 INDANYLOXY) 2 BUTANOL; ADRENALIN; ALPRENOLOL; BETA 2 ADRENERGIC RECEPTOR; BETA 2 ADRENERGIC RECEPTOR STIMULATING AGENT; CATECHOL; DOPAMINE; G PROTEIN COUPLED RECEPTOR; HALOSTACHINE; ISOPRENALINE; NORADRENALIN; RHODOPSIN; SALBUTAMOL; UNCLASSIFIED DRUG;

EID: 33746382921     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio801     Document Type: Article
Times cited : (312)

References (22)
  • 1
    • 0035800850 scopus 로고    scopus 로고
    • Activation of the beta 2-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 beta 2-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. Chem. , vol.276 , pp. 29171-29177
    • Ballesteros, J.A.1
  • 2
    • 0036239236 scopus 로고    scopus 로고
    • Mutagenesis and modelling of the alpha(1b)-adrenergic receptor highlight the role of the helix 3/helix 6 interface in receptor activation
    • Greasley, P.J., Fanelli, F., Rossier, O., Abuin, L. & Cotecchia, S. Mutagenesis and modelling of the alpha(1b)-adrenergic receptor highlight the role of the helix 3/helix 6 interface in receptor activation. Mol. Pharmacol. 61, 1025-1032 (2002).
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1025-1032
    • Greasley, P.J.1    Fanelli, F.2    Rossier, O.3    Abuin, L.4    Cotecchia, S.5
  • 3
    • 0037192858 scopus 로고    scopus 로고
    • Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A 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. Evidence for a model of agonist-induced activation of 5-hydroxytryptamine 2A serotonin receptors that involves the disruption of a strong ionic interaction between helices 3 and 6. J. Biol. Chem. 277, 11441-11449 (2002).
    • (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.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 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
  • 5
    • 0035816704 scopus 로고    scopus 로고
    • Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor
    • Ghanouni, P. et al. Functionally different agonists induce distinct conformations in the G protein coupling domain of the beta 2 adrenergic receptor. J. Biol. Chem. 276, 24433-24436 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 24433-24436
    • Ghanouni, P.1
  • 6
    • 0345791508 scopus 로고    scopus 로고
    • Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states
    • Swaminath, G. et al. Sequential binding of agonists to the beta2 adrenoceptor. Kinetic evidence for intermediate conformational states. J. Biol. Chem. 279, 686-691 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 686-691
    • Swaminath, G.1
  • 7
    • 20444499405 scopus 로고    scopus 로고
    • Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists
    • Swaminath, G. et al. Probing the beta2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 280, 22165-22171 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 22165-22171
    • Swaminath, G.1
  • 8
    • 0037176909 scopus 로고    scopus 로고
    • Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence
    • Mansoor, S.E., McHaourab, H.S. & Farrens, D.L. Mapping proximity within proteins using fluorescence spectroscopy. A study of T4 lysozyme showing that tryptophan residues quench bimane fluorescence. Biochemistry 41, 2475-2484 (2002).
    • (2002) Biochemistry , vol.41 , pp. 2475-2484
    • Mansoor, S.E.1    McHaourab, H.S.2    Farrens, D.L.3
  • 9
    • 0027519404 scopus 로고
    • A polymorphism of the human beta 2-adrenergic receptor within the fourth transmembrane domain alters ligand binding and functional properties of the receptor
    • Green, S.A., Cole, G., Jacinto, M., Innis, M. & Liggett, S.B. A polymorphism of the human beta 2-adrenergic receptor within the fourth transmembrane domain alters ligand binding and functional properties of the receptor. J. Biol. Chem. 268, 23116-23121 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 23116-23121
    • Green, S.A.1    Cole, G.2    Jacinto, M.3    Innis, M.4    Liggett, S.B.5
  • 10
    • 0037174606 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by a rotamer toggle switch
    • Shi, L. et al. Beta2 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
  • 11
    • 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. 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.5
  • 12
    • 20844434337 scopus 로고    scopus 로고
    • A FIAsH-based FRET approach to determine G protein-coupled receptor activation in living cells
    • Hoffmann, C. et al. A FIAsH-based FRET approach to determine G protein-coupled receptor activation in living cells. Nat. Methods 2, 171-176 (2005).
    • (2005) Nat. Methods , vol.2 , pp. 171-176
    • Hoffmann, C.1
  • 13
    • 29444444012 scopus 로고    scopus 로고
    • Molecular basis of inverse agonism in a G protein-coupled receptor
    • Vilardaga, J.P., Steinmeyer, R., Harms, G.S. & Lohse, M.J. Molecular basis of inverse agonism in a G protein-coupled receptor. Nat. Chem. Biol. 1, 25-28 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 25-28
    • Vilardaga, J.P.1    Steinmeyer, R.2    Harms, G.S.3    Lohse, M.J.4
  • 14
    • 26444467486 scopus 로고    scopus 로고
    • Linking agonist binding to histamine H1 receptor activation
    • Jongejan, A. et al. Linking agonist binding to histamine H1 receptor activation. Nat. Chem. Biol. 1, 98-103 (2005).
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 98-103
    • Jongejan, A.1
  • 16
    • 0030859541 scopus 로고    scopus 로고
    • Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor
    • Gether, U. et al. Agonists induce conformational changes in transmembrane domains III and VI of the beta2 adrenoceptor. EMBO J. 16, 6737-6747 (1997).
    • (1997) EMBO J. , vol.16 , pp. 6737-6747
    • Gether, U.1
  • 17
    • 0028809411 scopus 로고
    • Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor
    • Kobilka, B.K. Amino and carboxyl terminal modifications to facilitate the production and purification of a G protein-coupled receptor. Anal. Biochem. 231, 269-271 (1995).
    • (1995) Anal. Biochem. , vol.231 , pp. 269-271
    • Kobilka, B.K.1
  • 18
    • 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. & 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.1    Weinstein, H.2
  • 21
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein 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
  • 22
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E.A. & Bacon, D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.