메뉴 건너뛰기




Volumn 366, Issue 4, 2008, Pages 1001-1006

Functional role of the conserved proline in helix 6 of the human bradykinin B2 receptor

Author keywords

Activation; Bradykinin; G protein coupled receptor (GPCR); Mutagenesis; Proline

Indexed keywords

ALANINE; BRADYKININ B2 RECEPTOR; GLYCINE; GUANINE NUCLEOTIDE BINDING PROTEIN; LEUCINE; PROLINE;

EID: 37549037066     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.12.069     Document Type: Article
Times cited : (3)

References (30)
  • 1
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function
    • Kristiansen K. Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103 (2004) 21-80
    • (2004) Pharmacol. Ther. , vol.103 , pp. 21-80
    • Kristiansen, K.1
  • 3
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • Gether U. Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocrinol. Rev. 21 (2000) 90-113
    • (2000) Endocrinol. Rev. , vol.21 , pp. 90-113
    • Gether, U.1
  • 6
    • 36448995359 scopus 로고    scopus 로고
    • V. Cherezov, D.M. Rosenbaum, M.A. Hanson, S.G. Rasmussen, F.S. Thian, T.S. Kobilka, H.J. Choi, P. Kuhn, W.I. Weis, B.K. Kobilka, R.C. Stevens, High-resolution crystal structure of an engineered human {beta}2-adrenergic G protein coupled receptor, Science (2007).
  • 7
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: the role of prolines in signalling via transmembrane α-helices
    • Sansom M.S., and Weinstein H. Hinges, swivels and switches: the role of prolines in signalling via transmembrane α-helices. Trends Pharmacol. Sci. 21 (2000) 445-451
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 8
    • 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 (2001) 1-19
    • (2001) Mol. Pharmacol. , vol.60 , pp. 1-19
    • Ballesteros, J.A.1    Shi, L.2    Javitch, J.A.3
  • 9
    • 9144224914 scopus 로고    scopus 로고
    • Structural mimicry in class A G protein-coupled receptor rotamer toggle switches: the importance of the F3.36(201)/W6.48(357) interaction in cannabinoid CB1 receptor activation
    • McAllister S.D., Hurst D.P., Barnett-Norris J., Lynch D., Reggio P.H., and Abood M.E. Structural mimicry in class A G protein-coupled receptor rotamer toggle switches: the importance of the F3.36(201)/W6.48(357) interaction in cannabinoid CB1 receptor activation. J. Biol. Chem. 279 (2004) 48024-48037
    • (2004) J. Biol. Chem. , vol.279 , pp. 48024-48037
    • McAllister, S.D.1    Hurst, D.P.2    Barnett-Norris, J.3    Lynch, D.4    Reggio, P.H.5    Abood, M.E.6
  • 10
    • 0037174606 scopus 로고    scopus 로고
    • Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by rotamer toggle switch
    • Shi L., Liapakis G., Xu R., Guarnieri F., Ballesteros J.A., and Javitch J.A. Beta2 adrenergic receptor activation. Modulation of the proline kink in transmembrane 6 by rotamer toggle switch. J. Biol. Chem. 277 (2002) 40989-40996
    • (2002) J. Biol. Chem. , vol.277 , pp. 40989-40996
    • Shi, L.1    Liapakis, G.2    Xu, R.3    Guarnieri, F.4    Ballesteros, J.A.5    Javitch, J.A.6
  • 12
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzymatic reaction
    • Cheng Y., and Prusoff W.H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 percent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 22 (1973) 3099-3108
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 13
    • 10344255641 scopus 로고    scopus 로고
    • Mutations in the B2 bradykinin receptor reveal a different pattern of contacts for peptidic agonists and peptidic antagonists
    • Jarnagin K., Bhakta S., Zuppan P., Yee C., Ho T., Phan T., Tahilramani R., Pease J.H., Miller A., and Freedman R. Mutations in the B2 bradykinin receptor reveal a different pattern of contacts for peptidic agonists and peptidic antagonists. J. Biol. Chem. 271 (1996) 28277-28286
    • (1996) J. Biol. Chem. , vol.271 , pp. 28277-28286
    • Jarnagin, K.1    Bhakta, S.2    Zuppan, P.3    Yee, C.4    Ho, T.5    Phan, T.6    Tahilramani, R.7    Pease, J.H.8    Miller, A.9    Freedman, R.10
  • 16
    • 0027948084 scopus 로고
    • The effect of eight V2 vasopressin receptor mutations on stimulation of adenylyl cyclase and binding to vasopressin
    • Pan Y., Wilson P., and Gitschier J. The effect of eight V2 vasopressin receptor mutations on stimulation of adenylyl cyclase and binding to vasopressin. J. Biol. Chem. 269 (1994) 31933-31937
    • (1994) J. Biol. Chem. , vol.269 , pp. 31933-31937
    • Pan, Y.1    Wilson, P.2    Gitschier, J.3
  • 17
    • 0029046606 scopus 로고
    • Probing the "message:address" sites for chemoattractant binding to the C5a
    • Kolakowski Jr. L.F., Lu B., Gerard C., and Gerard N.P. Probing the "message:address" sites for chemoattractant binding to the C5a. J. Biol. Chem. 270 (1995) 18077-18082
    • (1995) J. Biol. Chem. , vol.270 , pp. 18077-18082
    • Kolakowski Jr., L.F.1    Lu, B.2    Gerard, C.3    Gerard, N.P.4
  • 18
    • 0036235905 scopus 로고    scopus 로고
    • The critical role of transmembrane prolines in human prostacyclin receptor activation
    • Stitham J., Martin K.A., and Hwa J. The critical role of transmembrane prolines in human prostacyclin receptor activation. Mol. Pharmacol. 61 (2002) 1202-1210
    • (2002) Mol. Pharmacol. , vol.61 , pp. 1202-1210
    • Stitham, J.1    Martin, K.A.2    Hwa, J.3
  • 19
    • 0029900790 scopus 로고    scopus 로고
    • Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-factor receptor
    • Konopka J.B., Margarit S.M., and Dube P. Mutation of Pro-258 in transmembrane domain 6 constitutively activates the G protein-coupled alpha-factor receptor. Proc. Natl. Acad. Sci. USA 93 (1996) 6764-6769
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6764-6769
    • Konopka, J.B.1    Margarit, S.M.2    Dube, P.3
  • 20
    • 13144265744 scopus 로고    scopus 로고
    • A constitutively active GPCR retains its G protein specificity and the ability to form dimers
    • Ladds G., Davis K., Das A., and Davey J. A constitutively active GPCR retains its G protein specificity and the ability to form dimers. Mol. Microbiol. 55 (2005) 482-497
    • (2005) Mol. Microbiol. , vol.55 , pp. 482-497
    • Ladds, G.1    Davis, K.2    Das, A.3    Davey, J.4
  • 21
    • 0034327611 scopus 로고    scopus 로고
    • Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices
    • Sansom M.S., and Weinstein H. Hinges, swivels and switches: the role of prolines in signalling via transmembrane alpha-helices. Trends Pharmacol. Sci. 21 (2000) 445-451
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 445-451
    • Sansom, M.S.1    Weinstein, H.2
  • 22
    • 0017868338 scopus 로고
    • Empirical predictions of protein conformation
    • Chou P.Y., and Fasman G.D. Empirical predictions of protein conformation. Annu. Rev. Biochem. 47 (1978) 251-276
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 23
    • 0031018485 scopus 로고    scopus 로고
    • Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility
    • Gether U., Ballesteros J.A., Seifert R., Sanders-Bush E., Weinstein H., and Kobilka B.K. Structural instability of a constitutively active G protein-coupled receptor. Agonist-independent activation due to conformational flexibility. J. Biol. Chem. 272 (1997) 2587-2590
    • (1997) J. Biol. Chem. , vol.272 , pp. 2587-2590
    • Gether, U.1    Ballesteros, J.A.2    Seifert, R.3    Sanders-Bush, E.4    Weinstein, H.5    Kobilka, B.K.6
  • 24
    • 0043235844 scopus 로고    scopus 로고
    • Ligand-selective receptor conformations revisited: the promise and the problem
    • Kenakin T. Ligand-selective receptor conformations revisited: the promise and the problem. Trends Pharmacol. Sci. 24 (2003) 346-354
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 346-354
    • Kenakin, T.1
  • 26
    • 0032747821 scopus 로고    scopus 로고
    • Effect of LF 16-0687MS, a new nonpeptide bradykinin B2 receptor antagonist, in a rat model of closed head trauma
    • Pruneau D., Chorny I., Benkovitz V., Artru A., Roitblat L., and Shapira Y. Effect of LF 16-0687MS, a new nonpeptide bradykinin B2 receptor antagonist, in a rat model of closed head trauma. J. Neurotrauma 16 (1999) 1057-1065
    • (1999) J. Neurotrauma , vol.16 , pp. 1057-1065
    • Pruneau, D.1    Chorny, I.2    Benkovitz, V.3    Artru, A.4    Roitblat, L.5    Shapira, Y.6
  • 27
    • 14544271929 scopus 로고    scopus 로고
    • Disulfide trapping to localize small-molecule agonists and antagonists for a G protein-coupled receptor
    • Buck E., and Wells J.A. Disulfide trapping to localize small-molecule agonists and antagonists for a G protein-coupled receptor. Proc. Natl. Acad. Sci. USA 102 (2005) 2719-2724
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2719-2724
    • Buck, E.1    Wells, J.A.2
  • 29
    • 1642331204 scopus 로고    scopus 로고
    • Site-directed mutagenesis at the human B2 receptor and molecular modelling to define the pharmacophore of non-peptide bradykinin receptor antagonists
    • Meini S., Cucchi P., Bellucci F., Catalani C., Faiella A., Rotondaro L., Quartara L., Giolitti A., and Maggi C.A. Site-directed mutagenesis at the human B2 receptor and molecular modelling to define the pharmacophore of non-peptide bradykinin receptor antagonists. Biochem. Pharmacol. 67 (2004) 601-609
    • (2004) Biochem. Pharmacol. , vol.67 , pp. 601-609
    • Meini, S.1    Cucchi, P.2    Bellucci, F.3    Catalani, C.4    Faiella, A.5    Rotondaro, L.6    Quartara, L.7    Giolitti, A.8    Maggi, C.A.9
  • 30
    • 0026755609 scopus 로고
    • Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains
    • Ballesteros J.A., and Weinstein H. Analysis and refinement of criteria for predicting the structure and relative orientations of transmembranal helical domains. Biophys. J. 62 (1992) 107-109
    • (1992) Biophys. J. , vol.62 , pp. 107-109
    • Ballesteros, J.A.1    Weinstein, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.