메뉴 건너뛰기




Volumn 289, Issue 27, 2014, Pages 18966-18977

Structural-functional analysis of the third transmembrane domain of the corticotropin-releasing factor type 1 receptor role in activation and allosteric antagonism

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; CHEMICAL ACTIVATION;

EID: 84903837647     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.544460     Document Type: Article
Times cited : (19)

References (31)
  • 1
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering ofGprotein-coupled receptors: An evolutionary success
    • Bockaert, J., and Pin, J. P. (1999) Molecular tinkering ofGprotein-coupled receptors: an evolutionary success. EMBO J. 18, 1723-1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 4
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch, V., Cherezov, V., and Stevens, R. C. (2013) Structure-function of the G protein-coupled receptor superfamily. Annu. Rev. Pharmacol. Toxicol. 53, 531-556
    • (2013) Annu. Rev. Pharmacol. Toxicol. , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3
  • 7
    • 16244383540 scopus 로고    scopus 로고
    • Mechanisms of peptide and nonpeptide ligand binding to Class B G protein-coupled receptors
    • Hoare, S. R. (2005) Mechanisms of peptide and nonpeptide ligand binding to Class B G protein-coupled receptors. Drug. Discov. Today 10, 417-427
    • (2005) Drug. Discov. Today , vol.10 , pp. 417-427
    • Hoare, S.R.1
  • 8
    • 0031764213 scopus 로고    scopus 로고
    • The first extracellular domain of corticotropin releasing factor-R1 contains major binding determinants for urocortin and astressin
    • Perrin, M. H., Sutton, S., Bain, D. L., Berggren, W. T., and Vale, W. W. (1998) The first extracellular domain of corticotropin releasing factor-R1 contains major binding determinants for urocortin and astressin. Endocrinology 139, 566-570
    • (1998) Endocrinology , vol.139 , pp. 566-570
    • Perrin, M.H.1    Sutton, S.2    Bain, D.L.3    Berggren, W.T.4    Vale, W.W.5
  • 11
    • 2442456104 scopus 로고    scopus 로고
    • A method for simultaneous alignment of multiple protein structures
    • Shatsky, M., Nussinov, R., and Wolfson, H. J. (2004) A method for simultaneous alignment of multiple protein structures. Proteins 56, 143-156
    • (2004) Proteins , vol.56 , pp. 143-156
    • Shatsky, M.1    Nussinov, R.2    Wolfson, H.J.3
  • 12
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M., Clamp, M., and Barton, G. J. (2009) Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 14
    • 77957225589 scopus 로고    scopus 로고
    • Exploring the binding site crevice of a family B G protein-coupled receptor, the type 1 corticotropin releasing factor receptor
    • Gkountelias, K., Papadokostaki, M., Javitch, J. A., and Liapakis, G. (2010) Exploring the binding site crevice of a family B G protein-coupled receptor, the type 1 corticotropin releasing factor receptor. Mol. Pharmacol. 78, 785-793
    • (2010) Mol. Pharmacol. , vol.78 , pp. 785-793
    • Gkountelias, K.1    Papadokostaki, M.2    Javitch, J.A.3    Liapakis, G.4
  • 15
    • 63849209885 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the second extracellular loop of type 1 corticotropinreleasing factor receptor revealed residues critical for peptide binding
    • Gkountelias, K., Tselios, T., Venihaki, M., Deraos, G., Lazaridis, I., Rassouli, O., Gravanis, A., and Liapakis, G. (2009) Alanine scanning mutagenesis of the second extracellular loop of type 1 corticotropinreleasing factor receptor revealed residues critical for peptide binding. Mol. Pharmacol. 75, 793-800
    • (2009) Mol. Pharmacol. , vol.75 , pp. 793-800
    • Gkountelias, K.1    Tselios, T.2    Venihaki, M.3    Deraos, G.4    Lazaridis, I.5    Rassouli, O.6    Gravanis, A.7    Liapakis, G.8
  • 16
    • 47049130668 scopus 로고    scopus 로고
    • Crystal structure of the ligand-free G protein-coupled receptor opsin
    • Park, J. H., Scheerer, P., Hofmann, K. P., Choe, H. W., and Ernst, O. P. (2008) Crystal structure of the ligand-free G protein-coupled receptor opsin. Nature 454, 183-187
    • (2008) Nature , vol.454 , pp. 183-187
    • Park, J.H.1    Scheerer, P.2    Hofmann, K.P.3    Choe, H.W.4    Ernst, O.P.5
  • 19
    • 77957055780 scopus 로고
    • Integrated methods for the construction of three-dimensional models of structure-function relations in G protein-coupled receptors
    • Ballesteros, J., and Weinstein, H. (1995) Integrated methods for the construction of three-dimensional models of structure-function relations in G protein-coupled receptors. Methods Neurosci. 25, 366-428
    • (1995) Methods Neurosci. , vol.25 , pp. 366-428
    • Ballesteros, J.1    Weinstein, H.2
  • 20
    • 0034792329 scopus 로고    scopus 로고
    • Use of the substituted cysteine accessibility method to study the structure and function of G proteincoupled receptors
    • Javitch, J. A., Shi, L., and Liapakis, G. (2002) Use of the substituted cysteine accessibility method to study the structure and function of G proteincoupled receptors. Methods Enzymol. 343, 137-156
    • (2002) Methods Enzymol. , vol.343 , pp. 137-156
    • Javitch, J.A.1    Shi, L.2    Liapakis, G.3
  • 21
    • 78751487961 scopus 로고    scopus 로고
    • A structural insight into the reorientation of transmembrane domains 3 and 5 during family A G proteincoupled receptor activation
    • Sansuk, K., Deupi, X., Torrecillas, I. R., Jongejan, A., Nijmeijer, S., Bakker, R. A., Pardo, L., and Leurs, R. (2011) A structural insight into the reorientation of transmembrane domains 3 and 5 during family A G proteincoupled receptor activation. Mol. Pharmacol. 79, 262-269
    • (2011) Mol. Pharmacol. , vol.79 , pp. 262-269
    • Sansuk, K.1    Deupi, X.2    Torrecillas, I.R.3    Jongejan, A.4    Nijmeijer, S.5    Bakker, R.A.6    Pardo, L.7    Leurs, R.8
  • 24
    • 77950195236 scopus 로고    scopus 로고
    • Identification of determinants of glucose-dependent insulinotropic polypeptide receptor that interact with N-terminal biologically active region of the natural ligand
    • Yaqub, T., Tikhonova, I. G., Lättig, J., Magnan, R., Laval, M., Escrieut, C., Boulègue, C., Hewage, C., and Fourmy, D. (2010) Identification of determinants of glucose-dependent insulinotropic polypeptide receptor that interact with N-terminal biologically active region of the natural ligand. Mol. Pharmacol. 77, 547-558
    • (2010) Mol. Pharmacol. , vol.77 , pp. 547-558
    • Yaqub, T.1    Tikhonova, I.G.2    Lättig, J.3    Magnan, R.4    Laval, M.5    Escrieut, C.6    Boulègue, C.7    Hewage, C.8    Fourmy, D.9
  • 25
    • 0033548654 scopus 로고    scopus 로고
    • The functional topography of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor, revealed by scanning mutagenesis
    • Lu, Z. L., and Hulme, E. C. (1999) The functional topography of transmembrane domain 3 of the M1 muscarinic acetylcholine receptor, revealed by scanning mutagenesis. J. Biol. Chem. 274, 7309-7315
    • (1999) J. Biol. Chem. , vol.274 , pp. 7309-7315
    • Lu, Z.L.1    Hulme, E.C.2
  • 26
    • 0029953735 scopus 로고    scopus 로고
    • A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor
    • Perlman, J. H., Laakkonen, L. J., Guarnieri, F., Osman, R., and Gershengorn, M. C. (1996) A refined model of the thyrotropin-releasing hormone (TRH) receptor binding pocket. Experimental analysis and energy minimization of the complex between TRH and TRH receptor. Biochemistry 35, 7643-7650
    • (1996) Biochemistry , vol.35 , pp. 7643-7650
    • Perlman, J.H.1    Laakkonen, L.J.2    Guarnieri, F.3    Osman, R.4    Gershengorn, M.C.5
  • 28
    • 0002769281 scopus 로고    scopus 로고
    • The CRF receptor: Structure, function and potential for therapeutic intervention
    • Grigoriadis, D. E., Haddach, M., Ling, N., and Saunders, J. (2001) The CRF receptor: structure, function and potential for therapeutic intervention. Curr. Med. Chem. Syst. Agents 1, 63-97
    • (2001) Curr. Med. Chem. Syst. Agents , vol.1 , pp. 63-97
    • Grigoriadis, D.E.1    Haddach, M.2    Ling, N.3    Saunders, J.4
  • 29
    • 0024314491 scopus 로고
    • CRH and -helical- CRH modulate behavioral measures of arousal in monkeys
    • Winslow, J. T., Newman, J. D., and Insel, T. R. (1989) CRH and -helical- CRH modulate behavioral measures of arousal in monkeys. Pharmacol. Biochem. Behav. 32, 919-926
    • (1989) Pharmacol. Biochem. Behav. , vol.32 , pp. 919-926
    • Winslow, J.T.1    Newman, J.D.2    Insel, T.R.3
  • 30
    • 0033020807 scopus 로고    scopus 로고
    • Comparison of an agonist, urocortin, and an antagonist, astressin, as radioligands for characterization of corticotropin-releasing factor receptors
    • Perrin, M. H., Sutton, S. W., Cervini, L. A., Rivier, J. E., and Vale, W. W. (1999) Comparison of an agonist, urocortin, and an antagonist, astressin, as radioligands for characterization of corticotropin-releasing factor receptors. J. Pharmacol. Exp. Ther. 288, 729-734
    • (1999) J. Pharmacol. Exp. Ther. , vol.288 , pp. 729-734
    • Perrin, M.H.1    Sutton, S.W.2    Cervini, L.A.3    Rivier, J.E.4    Vale, W.W.5
  • 31
    • 1542379652 scopus 로고    scopus 로고
    • Evolutionary trace of G protein-coupled receptors reveals clusters of residues that determine global and class-specific functions
    • Madabushi, S., Gross, A. K., Philippi, A., Meng, E. C., Wensel, T. G., and Lichtarge, O. (2004) Evolutionary trace of G protein-coupled receptors reveals clusters of residues that determine global and class-specific functions. J. Biol. Chem. 279, 8126-8132
    • (2004) J. Biol. Chem. , vol.279 , pp. 8126-8132
    • Madabushi, S.1    Gross, A.K.2    Philippi, A.3    Meng, E.C.4    Wensel, T.G.5    Lichtarge, O.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.