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Volumn 290, Issue 5, 2015, Pages 2870-2878

Determinants of endogenous ligand specificity divergence among metabotropic glutamate receptors

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BINDING SITES;

EID: 84921915382     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.622233     Document Type: Article
Times cited : (16)

References (28)
  • 1
    • 0030995878 scopus 로고    scopus 로고
    • Pharmacology and functions of metabotropic glutamate receptors
    • Conn, P. J., and Pin, J. P. (1997) Pharmacology and functions of metabotropic glutamate receptors. Annu. Rev. Pharmacol. Toxicol. 37, 205-237
    • (1997) Annu. Rev. Pharmacol. Toxicol. , vol.37 , pp. 205-237
    • Conn, P.J.1    Pin, J.P.2
  • 2
    • 0029913807 scopus 로고    scopus 로고
    • An evolutionary trace method defines binding surfaces common to protein families
    • Lichtarge, O., Bourne, H. R., and Cohen, F. E. (1996) An evolutionary trace method defines binding surfaces common to protein families. J. Mol. Biol. 257, 342-358
    • (1996) J. Mol. Biol. , vol.257 , pp. 342-358
    • Lichtarge, O.1    Bourne, H.R.2    Cohen, F.E.3
  • 3
    • 0034652331 scopus 로고    scopus 로고
    • Aregulator of G protein signaling interaction surface linked to effector specificity
    • Sowa, M. E., He, W., Wensel, T. G., and Lichtarge, O. (2000)Aregulator of G protein signaling interaction surface linked to effector specificity. Proc. Natl. Acad. Sci. U.S.A. 97, 1483-1488
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1483-1488
    • Sowa, M.E.1    He, W.2    Wensel, T.G.3    Lichtarge, O.4
  • 4
    • 0035126520 scopus 로고    scopus 로고
    • Prediction and confirmation of a site critical for effector regulation of RGS domain activity
    • Sowa, M. E., He, W., Slep, K. C., Kercher, M. A., Lichtarge, O., and Wensel, T. G. (2001) Prediction and confirmation of a site critical for effector regulation of RGS domain activity. Nat. Struct. Biol. 8, 234-237
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 234-237
    • Sowa, M.E.1    He, W.2    Slep, K.C.3    Kercher, M.A.4    Lichtarge, O.5    Wensel, T.G.6
  • 5
    • 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
  • 6
    • 77952356281 scopus 로고    scopus 로고
    • Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors
    • Rodriguez, G. J., Yao, R., Lichtarge, O., and Wensel, T. G. (2010) Evolution-guided discovery and recoding of allosteric pathway specificity determinants in psychoactive bioamine receptors. Proc. Natl. Acad. Sci. U.S.A. 107, 7787-7792
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 7787-7792
    • Rodriguez, G.J.1    Yao, R.2    Lichtarge, O.3    Wensel, T.G.4
  • 8
    • 67649951498 scopus 로고    scopus 로고
    • Functional rescue of β-adrenoceptor dimerization and trafficking by pharmacological chaperones
    • Kobayashi, H., Ogawa, K., Yao, R., Lichtarge, O., and Bouvier, M. (2009) Functional rescue of β-adrenoceptor dimerization and trafficking by pharmacological chaperones. Traffic 10, 1019-1033
    • (2009) Traffic , vol.10 , pp. 1019-1033
    • Kobayashi, H.1    Ogawa, K.2    Yao, R.3    Lichtarge, O.4    Bouvier, M.5
  • 9
    • 84908191816 scopus 로고    scopus 로고
    • Selectivity and evolutionary divergence of metabotropic glutamate receptors for endogenous ligands and G proteins coupled to phospholipase C or TRP channels
    • Kang, H. J., Menlove, K., Ma, J., Wilkins, A., Lichtarge, O., and Wensel, T. G. (2014) Selectivity and evolutionary divergence of metabotropic glutamate receptors for endogenous ligands and G proteins coupled to phospholipase C or TRP channels. J. Biol. Chem. 289, 29961-29974
    • (2014) J. Biol. Chem. , vol.289 , pp. 29961-29974
    • Kang, H.J.1    Menlove, K.2    Ma, J.3    Wilkins, A.4    Lichtarge, O.5    Wensel, T.G.6
  • 10
    • 1242339659 scopus 로고    scopus 로고
    • A family of evolution-entropy hybrid methods for ranking protein residues by importance
    • Mihalek, I., Res, I., and Lichtarge, O. (2004) A family of evolution-entropy hybrid methods for ranking protein residues by importance. J. Mol. Biol. 336, 1265-1282
    • (2004) J. Mol. Biol. , vol.336 , pp. 1265-1282
    • Mihalek, I.1    Res, I.2    Lichtarge, O.3
  • 11
    • 84886063889 scopus 로고    scopus 로고
    • Accounting for epistatic interactions improves the functional analysis of protein structures
    • Wilkins, A. D., Venner, E., Marciano, D. C., Erdin, S., Atri, B., Lua, R. C., and Lichtarge, O. (2013) Accounting for epistatic interactions improves the functional analysis of protein structures. Bioinformatics 29, 2714-2721
    • (2013) Bioinformatics , vol.29 , pp. 2714-2721
    • Wilkins, A.D.1    Venner, E.2    Marciano, D.C.3    Erdin, S.4    Atri, B.5    Lua, R.C.6    Lichtarge, O.7
  • 12
    • 0037022586 scopus 로고    scopus 로고
    • Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+
    • Tsuchiya, D., Kunishima, N., Kamiya, N., Jingami, H., and Morikawa, K. (2002) Structural views of the ligand-binding cores of a metabotropic glutamate receptor complexed with an antagonist and both glutamate and Gd3+. Proc. Natl. Acad. Sci. U.S.A. 99, 2660-2665
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 2660-2665
    • Tsuchiya, D.1    Kunishima, N.2    Kamiya, N.3    Jingami, H.4    Morikawa, K.5
  • 13
    • 42449090264 scopus 로고    scopus 로고
    • PROMALS3D: A tool for multiple protein sequence and structure alignments
    • Pei, J., Kim, B. H., and Grishin, N. V. (2008) PROMALS3D: a tool for multiple protein sequence and structure alignments. Nucleic Acids Res. 36, 2295-2300
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2295-2300
    • Pei, J.1    Kim, B.H.2    Grishin, N.V.3
  • 15
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 16
    • 84865263040 scopus 로고    scopus 로고
    • Functional and pharmacological characteristics of metabotropic glutamate receptors 2/4 heterodimers
    • Kammermeier, P. J. (2012) Functional and pharmacological characteristics of metabotropic glutamate receptors 2/4 heterodimers. Mol. Pharmacol. 82, 438-447
    • (2012) Mol. Pharmacol. , vol.82 , pp. 438-447
    • Kammermeier, P.J.1
  • 18
    • 34247210665 scopus 로고    scopus 로고
    • Structures of the extracellular regions of the group II/III metabotropic glutamate receptors
    • Muto, T., Tsuchiya, D., Morikawa, K., and Jingami, H. (2007) Structures of the extracellular regions of the group II/III metabotropic glutamate receptors. Proc. Natl. Acad. Sci. U.S.A. 104, 3759-3764
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 3759-3764
    • Muto, T.1    Tsuchiya, D.2    Morikawa, K.3    Jingami, H.4
  • 20
    • 0037423395 scopus 로고    scopus 로고
    • Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state
    • Sato, T., Shimada, Y., Nagasawa, N., Nakanishi, S., and Jingami, H. (2003) Amino acid mutagenesis of the ligand binding site and the dimer interface of the metabotropic glutamate receptor 1. Identification of crucial residues for setting the activated state. J. Biol. Chem. 278, 4314-4321
    • (2003) J. Biol. Chem. , vol.278 , pp. 4314-4321
    • Sato, T.1    Shimada, Y.2    Nagasawa, N.3    Nakanishi, S.4    Jingami, H.5
  • 21
    • 84898993517 scopus 로고    scopus 로고
    • The ensemble nature of allostery
    • Motlagh, H. N., Wrabl, J. O., Li, J., and Hilser, V. J. (2014) The ensemble nature of allostery. Nature 508, 331-339
    • (2014) Nature , vol.508 , pp. 331-339
    • Motlagh, H.N.1    Wrabl, J.O.2    Li, J.3    Hilser, V.J.4
  • 22
    • 84895745240 scopus 로고    scopus 로고
    • Aunified view of "how allostery works."
    • Tsai, C. J., and Nussinov, R. (2014)Aunified view of "how allostery works." PLoS Comput. Biol. 10, e1003394
    • (2014) PLoS Comput. Biol. , vol.10 , pp. e1003394
    • Tsai, C.J.1    Nussinov, R.2
  • 23
    • 0035818605 scopus 로고    scopus 로고
    • Positive allosteric modulators of metabotropic glutamate 1 receptor: Characterization, mechanism of action, and binding site
    • Knoflach, F., Mutel, V., Jolidon, S., Kew, J. N., Malherbe, P., Vieira, E., Wichmann, J., and Kemp, J. A. (2001) Positive allosteric modulators of metabotropic glutamate 1 receptor: characterization, mechanism of action, and binding site. Proc. Natl. Acad. Sci. U.S.A. 98, 13402-13407
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13402-13407
    • Knoflach, F.1    Mutel, V.2    Jolidon, S.3    Kew, J.N.4    Malherbe, P.5    Vieira, E.6    Wichmann, J.7    Kemp, J.A.8
  • 24
    • 0037363728 scopus 로고    scopus 로고
    • Positive allosteric modulation of the human metabotropic glutamate receptor 4 (hmGluR4) by SIB-1893 and MPEP
    • Mathiesen, J. M., Svendsen, N., Bräuner-Osborne, H., Thomsen, C., and Ramirez, M. T. (2003) Positive allosteric modulation of the human metabotropic glutamate receptor 4 (hmGluR4) by SIB-1893 and MPEP. Br. J. Pharmacol. 138, 1026-1030
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 1026-1030
    • Mathiesen, J.M.1    Svendsen, N.2    Bräuner-Osborne, H.3    Thomsen, C.4    Ramirez, M.T.5
  • 28
    • 49949084014 scopus 로고    scopus 로고
    • Allosteric potentiators of metabotropic glutamate receptor subtype 1a differentially modulate independent signaling pathways in baby hamster kidney cells
    • Sheffler, D. J., and Conn, P. J. (2008) Allosteric potentiators of metabotropic glutamate receptor subtype 1a differentially modulate independent signaling pathways in baby hamster kidney cells. Neuropharmacology 55, 419-427
    • (2008) Neuropharmacology , vol.55 , pp. 419-427
    • Sheffler, D.J.1    Conn, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.