메뉴 건너뛰기




Volumn 44, Issue 31, 2005, Pages 10593-10604

Structural and molecular characterization of a preferred protein interaction surface on G protein βγ subunits

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ENERGY; AMINO ACIDS; BINDING ENERGY; CELL CULTURE; MIXTURES; MOLECULAR STRUCTURE; MUTAGENESIS; POLYPEPTIDES;

EID: 23244449285     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050655i     Document Type: Article
Times cited : (69)

References (41)
  • 1
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A. G. (1987) G proteins: transducers of receptor-generated signals, Annu. Rev. Biochem. 56, 615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 2
    • 0031984517 scopus 로고    scopus 로고
    • The many faces of G protein signaling
    • Hamm, H. E. (1998) The many faces of G protein signaling, J. Biol. Chem. 273, 669-672.
    • (1998) J. Biol. Chem. , vol.273 , pp. 669-672
    • Hamm, H.E.1
  • 6
    • 0032568664 scopus 로고    scopus 로고
    • Sites for G-α binding on the G protein β subunit overlap with sites for regulation of phospholipase C β and adenylyl cyclase
    • Li, Y., Sternweis, P. M., Charnecki, S., Smith, T. F., Gilman, A. G., Neer, E. J., and Kozasa, T. (1998) Sites for G-α binding on the G protein β subunit overlap with sites for regulation of phospholipase C β and adenylyl cyclase, J. Biol. Chem. 273, 16265-16272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16265-16272
    • Li, Y.1    Sternweis, P.M.2    Charnecki, S.3    Smith, T.F.4    Gilman, A.G.5    Neer, E.J.6    Kozasa, T.7
  • 8
    • 0034254946 scopus 로고    scopus 로고
    • Role of C-terminal domains of the G protein β subunit in the activation of effectors
    • Myung, C. S., and Garrison, J. C. (2000) Role of C-terminal domains of the G protein β subunit in the activation of effectors, Proc. Natl. Acad. Sci. U.S.A. 97, 9311-9316.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9311-9316
    • Myung, C.S.1    Garrison, J.C.2
  • 9
    • 0035815732 scopus 로고    scopus 로고
    • Characterization of a phospholipase C β2-binding site near the amino terminal coiled-coil of G protein βγ subunits
    • Yoshikawa, D. M., Bresciano, K., Hatwar, M., and Smrcka, A. V. (2001) Characterization of a phospholipase C β2-binding site near the amino terminal coiled-coil of G protein βγ subunits, J. Biol. Chem. 276, 11246-11251.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11246-11251
    • Yoshikawa, D.M.1    Bresciano, K.2    Hatwar, M.3    Smrcka, A.V.4
  • 10
    • 0035865394 scopus 로고    scopus 로고
    • Evidence that a protein-protein interaction "hot spot" on heterotrimeric G protein βγ subunits is used for recognition of a subclass of effectors
    • Scott, J. K., Huang, S. F., Gangadhar, B. P., Samoriski, G. M., Clapp, P., Gross, R. A., Taussig, R., and Smrcka, A. V. (2001) Evidence that a protein-protein interaction "hot spot" on heterotrimeric G protein βγ subunits is used for recognition of a subclass of effectors, EMBO J. 20, 767-776.
    • (2001) EMBO J. , vol.20 , pp. 767-776
    • Scott, J.K.1    Huang, S.F.2    Gangadhar, B.P.3    Samoriski, G.M.4    Clapp, P.5    Gross, R.A.6    Taussig, R.7    Smrcka, A.V.8
  • 11
    • 0036469060 scopus 로고    scopus 로고
    • Unraveling hot spots in binding interfaces: Progress and challenges
    • Delano, W. L. (2002) Unraveling hot spots in binding interfaces: progress and challenges, Curr. Opin. Struct. Biol. 12, 14-20.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 14-20
    • Delano, W.L.1
  • 12
    • 0035366379 scopus 로고    scopus 로고
    • Protein functional libraries: Hot spots, dynamics and combinatorial libraires
    • Ma, B., Wolfson, H. J., and Nussinov, R. (2001) Protein functional libraries: hot spots, dynamics and combinatorial libraires, Curr. Opin. Struct. Biol. 11, 364-369.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 364-369
    • Ma, B.1    Wolfson, H.J.2    Nussinov, R.3
  • 13
    • 15444366833 scopus 로고    scopus 로고
    • Regulatory interactions between the amino terminus of G-protein βγ subunits and the catalytic domain of PLCβ2
    • Bonacci, T. M., Ghosh, M., Malik, S., and Smrcka, A. V. (2005) Regulatory interactions between the amino terminus of G-protein βγ subunits and the catalytic domain of PLCβ2, J. Biol. Chem. 280, 10174-10181.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10174-10181
    • Bonacci, T.M.1    Ghosh, M.2    Malik, S.3    Smrcka, A.V.4
  • 14
    • 0037827724 scopus 로고    scopus 로고
    • Stimulation of cellular signaling and G protein subunit dissociation by G protein βγ subunit binding peptides
    • Goubaeva, F., Ghosh, M., Malik, S., Yang, J., Hinkle, P. M., Griendling, K. K., Neubig, R. R., and Smrcka, A. V. (2003) Stimulation of cellular signaling and G protein subunit dissociation by G protein βγ subunit binding peptides, J. Biol. Chem. 278, 19634-19641.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19634-19641
    • Goubaeva, F.1    Ghosh, M.2    Malik, S.3    Yang, J.4    Hinkle, P.M.5    Griendling, K.K.6    Neubig, R.R.7    Smrcka, A.V.8
  • 15
    • 0041315914 scopus 로고    scopus 로고
    • Receptor and nucleotide exchange independent mechanisms for promoting G protein subunit dissociation
    • Ghosh, M., Peterson, Y. K., Lanier, S. M., and Smrcka, A. V. (2003) Receptor and nucleotide exchange independent mechanisms for promoting G protein subunit dissociation, J. Biol. Chem. 273, 34747-34750.
    • (2003) J. Biol. Chem. , vol.273 , pp. 34747-34750
    • Ghosh, M.1    Peterson, Y.K.2    Lanier, S.M.3    Smrcka, A.V.4
  • 16
    • 0029662023 scopus 로고    scopus 로고
    • G-β subunit interacts with a peptide encoding region 956-982 of adenylyl cyclase 2: Cross-linking of the peptide to free G βγ but not the heterotrimer
    • Weng, G. Z., Li, J. R., Dingus, J., Hildebrandt, J. D., Weinstein, H., and Iyengar, R. (1996) G-β subunit interacts with a peptide encoding region 956-982 of adenylyl cyclase 2: Cross-linking of the peptide to free G βγ but not the heterotrimer, J. Biol. Chem. 271, 26445-26448.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26445-26448
    • Weng, G.Z.1    Li, J.R.2    Dingus, J.3    Hildebrandt, J.D.4    Weinstein, H.5    Iyengar, R.6
  • 18
    • 0027481032 scopus 로고
    • The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase
    • Koch, W. J., Inglese, J., Stone, W. C., and Lefkowitz, R. J. (1993) The binding site for the βγ subunits of heterotrimeric G proteins on the β-adrenergic receptor kinase, J. Biol. Chem. 268, 8256-8260.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8256-8260
    • Koch, W.J.1    Inglese, J.2    Stone, W.C.3    Lefkowitz, R.J.4
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode, Macromol
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Macromol. Crystallogr., Part A 276, 307-326.
    • (1997) Crystallogr., Part A , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 22
    • 0035788107 scopus 로고    scopus 로고
    • Pushing the boundaries of molecular replacement with maximum likelihood
    • Read, R. (2001) Pushing the boundaries of molecular replacement with maximum likelihood, Acta Crystallogr., Sect. D: Biol. Crystallogr. 57, 1373-1382.
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.57 , pp. 1373-1382
    • Read, R.1
  • 24
    • 0030986177 scopus 로고    scopus 로고
    • Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement, Proc
    • Adams, P. D., Pannu, N. S., Read, R. J., and Brunger, A. T. (1997) Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement, Proc. Natl. Acad. Sci U.S.A. 94, 5018-5023.
    • (1997) Natl. Acad. Sci U.S.A. , vol.94 , pp. 5018-5023
    • Adams, P.D.1    Pannu, N.S.2    Read, R.J.3    Brunger, A.T.4
  • 25
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron-density maps and the location of errors in these models, Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 26
    • 0000243829 scopus 로고
    • Procheck-A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., Macarthur, M. W., Moss, D. S., and Thornton, J. M. (1993) Procheck-A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 27
    • 0035719155 scopus 로고    scopus 로고
    • Discovery of ligands for βγ subunits from phage-displayed peptide libraries
    • Smrcka, A. V., and Scott, J. K. (2002) Discovery of ligands for βγ subunits from phage-displayed peptide libraries, Methods Enzymol. 344, 557-576.
    • (2002) Methods Enzymol. , vol.344 , pp. 557-576
    • Smrcka, A.V.1    Scott, J.K.2
  • 28
    • 0032478355 scopus 로고    scopus 로고
    • Determinants of Giα and βγ binding: Measuring high affinity interactions in a lipid environment using flow cytometry
    • Sarvazyan, N. A., Remmers, A. E., and Neubig, R. R. (1998) Determinants of Giα and βγ binding: Measuring high affinity interactions in a lipid environment using flow cytometry, J. Biol. Chem. 273, 7934-7940.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7934-7940
    • Sarvazyan, N.A.1    Remmers, A.E.2    Neubig, R.R.3
  • 29
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein βγ dimer at 2.1 A resolution
    • Sondek, J., Bohm, A., Lambright, D. G., Hamm, H. E., and Sigler, P. B. (1996) Crystal structure of a G-protein βγ dimer at 2.1 A resolution, Nature 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 31
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 angstroms resolution of the complex of transducin βγ and its regulator, phosducin
    • Gaudet, R., Bohm, A., and Sigler, P. B. (1996) Crystal structure at 2.4 angstroms resolution of the complex of transducin βγ and its regulator, phosducin, Cell 87, 577-588.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 32
    • 0032528863 scopus 로고    scopus 로고
    • Phosducin induces a structural change in transducin βγ
    • Loew, A., Ho, Y. K., Blundell, T., and Bax, B. (1998) Phosducin induces a structural change in transducin βγ, Structure 6, 1007-1019.
    • (1998) Structure , vol.6 , pp. 1007-1019
    • Loew, A.1    Ho, Y.K.2    Blundell, T.3    Bax, B.4
  • 34
    • 0037799206 scopus 로고    scopus 로고
    • Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gβγ
    • Lodowski, D. T., Pitcher, J. A., Capel, W. D., Lefkowitz, R. J., and Tesmer, J. J. G. (2003) Keeping G proteins at bay: A complex between G protein-coupled receptor kinase 2 and Gβγ, Science 300, 1256-1262.
    • (2003) Science , vol.300 , pp. 1256-1262
    • Lodowski, D.T.1    Pitcher, J.A.2    Capel, W.D.3    Lefkowitz, R.J.4    Tesmer, J.J.G.5
  • 35
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A. A., and Thorn, K. S. (1998) Anatomy of hot spots in protein interfaces, J. Mol. Biol. 280, 1-9.
    • (1998) J. Mol. Biol. , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 36
    • 0028916599 scopus 로고
    • A hot-spot of binding-energy in a hormone-receptor interface
    • Clackson, T., and Wells, J. A. (1995) A hot-spot of binding-energy in a hormone-receptor interface, Science 267, 383-386.
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 37
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • Delano, W. L., Ultsch, M. H., de Vos, A. M., and Wells, J. A. (2000) Convergent solutions to binding at a protein-protein interface, Science 287, 1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • Delano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 38
    • 0042377360 scopus 로고    scopus 로고
    • Mutagenesis of the runt domain defines two energetic hot spots for heterodimerization with the core binding factor β subunit
    • Zhang, L., Li, Z., Yan, J., Pradhan, P., Corpora, T., Cheney, M. D., Bravo, J., Warren, A. J., Bushweller, J. H., and Speck, N. A. (2003) Mutagenesis of the runt domain defines two energetic hot spots for heterodimerization with the core binding factor β subunit, J. Biol. Chem. 278, 33097-33104.
    • (2003) J. Biol. Chem. , vol.278 , pp. 33097-33104
    • Zhang, L.1    Li, Z.2    Yan, J.3    Pradhan, P.4    Corpora, T.5    Cheney, M.D.6    Bravo, J.7    Warren, A.J.8    Bushweller, J.H.9    Speck, N.A.10
  • 40
    • 0032530652 scopus 로고    scopus 로고
    • Structural basis of activity and subunit recognition in g protein heterotrimers
    • Wall, M., Posner, B., and Sprang, S. (1998) Structural basis of activity and subunit recognition in g protein heterotrimers, Structure 6, 1169-1183.
    • (1998) Structure , vol.6 , pp. 1169-1183
    • Wall, M.1    Posner, B.2    Sprang, S.3
  • 41
    • 0037566361 scopus 로고    scopus 로고
    • Custom distinctions in the interaction of G-protein β subunits with N-type (CaV2.2) versus P/Q-type (CaV2.1 ) calcium channels
    • Agler, H. L., Evans, J., Colecraft, H. M., and Yue, D. T. (2003) Custom distinctions in the interaction of G-protein β subunits with N-type (CaV2.2) versus P/Q-type (CaV2.1 ) calcium channels, J. Gen. Physiol. 121, 495-510.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 495-510
    • Agler, H.L.1    Evans, J.2    Colecraft, H.M.3    Yue, D.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.