메뉴 건너뛰기




Volumn 341, Issue 1, 2004, Pages 93-106

Dynamic coupling between the SH2 domain and active site of the COOH terminal Src kinase, Csk

Author keywords

AMPPNP, 5 adenylyl imidodiphosphate; Csk; Csk, COOH terminal Src kinase; deuterium exchange; DXMS, hydrogen deuterium exchange mass spectrometry; ESI, electrospray ionization; H D, hydrogen deuterium; kinase; mass spectrometry; stopped flow

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALANINE; DEUTERIUM; GLYCINE; HYDROGEN; PROTEIN SH2; PROTEIN TYROSINE KINASE; TYROSINE;

EID: 4143118969     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.060     Document Type: Article
Times cited : (39)

References (36)
  • 3
    • 0033600568 scopus 로고    scopus 로고
    • Domain interactions in protein tyrosine kinase Csk
    • Sondhi D., Cole P.A. Domain interactions in protein tyrosine kinase Csk. Biochemistry. 38:1999;11147-11155
    • (1999) Biochemistry , vol.38 , pp. 11147-11155
    • Sondhi, D.1    Cole, P.A.2
  • 4
    • 0025211917 scopus 로고
    • Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src
    • Hirai H., Varmus H.E. Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src. Mol. Cell. Biol. 10:1990;1307-1318
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1307-1318
    • Hirai, H.1    Varmus, H.E.2
  • 5
    • 0033566180 scopus 로고    scopus 로고
    • Mutations in the N-terminal regulatory region reduce the catalytic activity of Csk, but do not affect its recognition of Src
    • Sun G., Budde R.J. Mutations in the N-terminal regulatory region reduce the catalytic activity of Csk, but do not affect its recognition of Src. Arch. Biochem. Biophys. 367:1999;167-172
    • (1999) Arch. Biochem. Biophys. , vol.367 , pp. 167-172
    • Sun, G.1    Budde, R.J.2
  • 6
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F., Moarefi I., Kuriyan J. Crystal structure of the Src family tyrosine kinase Hck. Nature. 385:1997;602-609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 7
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature. 385:1997;595-602
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 8
    • 0026572318 scopus 로고
    • Effects of SH2 and SH3 deletions on the functional activities of wild- type and transforming variants of c-Src
    • Seidel-Dugan C., Meyer B.E., Thomas S.M., Brugge J.S. Effects of SH2 and SH3 deletions on the functional activities of wild- type and transforming variants of c-Src. Mol. Cell. Biol. 12:1992;1835-1845
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1835-1845
    • Seidel-Dugan, C.1    Meyer, B.E.2    Thomas, S.M.3    Brugge, J.S.4
  • 10
    • 0035900556 scopus 로고    scopus 로고
    • Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: Insights from NMR mapping studies and site-directed mutagenesis
    • Shekhtman A., Ghose R., Wang D., Cole P.A., Cowburn D. Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis. J. Mol. Biol. 314:2001;129-138
    • (2001) J. Mol. Biol. , vol.314 , pp. 129-138
    • Shekhtman, A.1    Ghose, R.2    Wang, D.3    Cole, P.A.4    Cowburn, D.5
  • 12
    • 0035909107 scopus 로고    scopus 로고
    • Nucleotide release and associated conformational changes regulate function in the cooh-terminal src kinase, csk
    • Shaffer J., Sun G., Adams J.A. Nucleotide release and associated conformational changes regulate function in the cooh-terminal src kinase, csk. Biochemistry. 40:2001;11149-11155
    • (2001) Biochemistry , vol.40 , pp. 11149-11155
    • Shaffer, J.1    Sun, G.2    Adams, J.A.3
  • 13
    • 0036428762 scopus 로고    scopus 로고
    • Phosphorylation driven motions in the COOH-terminal Src kinase, Csk, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS)
    • Hamuro Y., Wong L., Shaffer J., Kim J.S., Stranz D.D., Jennings P.A., et al. Phosphorylation driven motions in the COOH-terminal Src kinase, Csk, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS). J. Mol. Biol. 323:2002;871-881
    • (2002) J. Mol. Biol. , vol.323 , pp. 871-881
    • Hamuro, Y.1    Wong, L.2    Shaffer, J.3    Kim, J.S.4    Stranz, D.D.5    Jennings, P.A.6
  • 14
    • 0038695015 scopus 로고    scopus 로고
    • Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK
    • Mikkola E.T., Bergman M. Conserved hydrophobicity in the SH2-kinase linker is required for catalytic activity of Csk and CHK. FEBS Letters. 544:2003;11-14
    • (2003) FEBS Letters , vol.544 , pp. 11-14
    • Mikkola, E.T.1    Bergman, M.2
  • 15
    • 0242424149 scopus 로고    scopus 로고
    • Novel destabilization of nucleotide binding by the gamma phosphate of ATP in the yeast SR protein kinase Sky1p
    • Aubol B.E., Nolen B., Shaffer J., Ghosh G., Adams J.A. Novel destabilization of nucleotide binding by the gamma phosphate of ATP in the yeast SR protein kinase Sky1p. Biochemistry. 42:2003;12813-12820
    • (2003) Biochemistry , vol.42 , pp. 12813-12820
    • Aubol, B.E.1    Nolen, B.2    Shaffer, J.3    Ghosh, G.4    Adams, J.A.5
  • 16
    • 0037180380 scopus 로고    scopus 로고
    • Probing the nucleotide binding domain of the osmoregulator EnvZ using fluorescent nucleotide derivatives
    • Plesniak L., Horiuchi Y., Sem D., Meinenger D., Stiles L., Shaffer J., et al. Probing the nucleotide binding domain of the osmoregulator EnvZ using fluorescent nucleotide derivatives. Biochemistry. 41:2002;13876-13882
    • (2002) Biochemistry , vol.41 , pp. 13876-13882
    • Plesniak, L.1    Horiuchi, Y.2    Sem, D.3    Meinenger, D.4    Stiles, L.5    Shaffer, J.6
  • 17
    • 0033815252 scopus 로고    scopus 로고
    • Insights into nucleotide binding in protein kinase a using fluorescent adenosine derivatives
    • Ni Q., Shaffer J., Adams J.A. Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives. Protein Sci. 9:2000;1818-1827
    • (2000) Protein Sci. , vol.9 , pp. 1818-1827
    • Ni, Q.1    Shaffer, J.2    Adams, J.A.3
  • 18
    • 0034663983 scopus 로고    scopus 로고
    • Insights into the HER-2 receptor tyrosine kinase mechanism and substrate specificity using a transient kinetic analysis
    • Jan A.Y., Johnson E.F., Diamonti A.J., Carraway I.K., Anderson K.S. Insights into the HER-2 receptor tyrosine kinase mechanism and substrate specificity using a transient kinetic analysis. Biochemistry. 39:2000;9786-9803
    • (2000) Biochemistry , vol.39 , pp. 9786-9803
    • Jan, A.Y.1    Johnson, E.F.2    Diamonti, A.J.3    Carraway, I.K.4    Anderson, K.S.5
  • 19
    • 0030888270 scopus 로고    scopus 로고
    • Interactions of cyclins with cyclin-dependent kinases: A common interactive mechanism
    • Heitz F., Morris M.C., Fesquet D., Cavadore J.C., Doree M., Divita G. Interactions of cyclins with cyclin-dependent kinases: a common interactive mechanism. Biochemistry. 36:1997;4995-5003
    • (1997) Biochemistry , vol.36 , pp. 4995-5003
    • Heitz, F.1    Morris, M.C.2    Fesquet, D.3    Cavadore, J.C.4    Doree, M.5    Divita, G.6
  • 20
    • 0642315208 scopus 로고
    • Transient-state kinetic analysis of enzyme reaction pathways
    • Sigman D.S. 3rd edit. San Diego, CA: Academic Press
    • Johnson K.A. Transient-state kinetic analysis of enzyme reaction pathways. Sigman D.S. 3rd edit. The Enzymes. vol. 20:1992;2-61 Academic Press, San Diego, CA
    • (1992) The Enzymes , vol.20 , pp. 2-61
    • Johnson, K.A.1
  • 21
    • 0020674810 scopus 로고
    • New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes
    • Hiratsuka T. New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta. 742:1983;496-508
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 496-508
    • Hiratsuka, T.1
  • 22
    • 0026018966 scopus 로고
    • Kinetics of the interaction of 2′(3′)-O-(N- methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: Characterization of two acto-S1-ADP complexes
    • Woodward S.K., Eccleston J.F., Geeves M.A. Kinetics of the interaction of 2′(3′)-O-(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1: characterization of two acto-S1-ADP complexes. Biochemistry. 30:1991;422-430
    • (1991) Biochemistry , vol.30 , pp. 422-430
    • Woodward, S.K.1    Eccleston, J.F.2    Geeves, M.A.3
  • 23
    • 0035044995 scopus 로고    scopus 로고
    • Conformational change of proteins arising from normal mode calculations
    • Tama F., Sanejouand Y.H. Conformational change of proteins arising from normal mode calculations. Protein Eng. 14:2001;1-6
    • (2001) Protein Eng. , vol.14 , pp. 1-6
    • Tama, F.1    Sanejouand, Y.H.2
  • 24
    • 0242268469 scopus 로고    scopus 로고
    • Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins
    • Miyashita O., Onuchic J.N., Wolynes P.G. Nonlinear elasticity, proteinquakes, and the energy landscapes of functional transitions in proteins. Proc. Natl Acad. Sci. USA. 100:2003;12570-12575
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12570-12575
    • Miyashita, O.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 25
    • 0033628016 scopus 로고    scopus 로고
    • Kinases of the Src family: Structure and functions
    • Tatosyan A.G., Mizenina O.A. Kinases of the Src family: structure and functions. Biochemistry (Mosc). 65:2000;49-58
    • (2000) Biochemistry (Mosc) , vol.65 , pp. 49-58
    • Tatosyan, A.G.1    Mizenina, O.A.2
  • 26
    • 0027408171 scopus 로고
    • Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
    • Zheng J., Knighton D.R., Ten Eyck L.F., Karlsson R., Xuong N., Taylor S.S., Sowadski J.M. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor. Biochemistry. 32:1993;2154-2161
    • (1993) Biochemistry , vol.32 , pp. 2154-2161
    • Zheng, J.1    Knighton, D.R.2    Ten Eyck, L.F.3    Karlsson, R.4    Xuong, N.5    Taylor, S.S.6    Sowadski, J.M.7
  • 27
    • 0029644732 scopus 로고
    • Two structures of the catalytic domain of phosphorylase kinase: An active protein kinase complexed with substrate analogue and product
    • Owen D.J., Noble M.E., Garman E.F., Papageorgiou A.C., Johnson L.N. Two structures of the catalytic domain of phosphorylase kinase: an active protein kinase complexed with substrate analogue and product. Structure. 3:1995;467-482
    • (1995) Structure , vol.3 , pp. 467-482
    • Owen, D.J.1    Noble, M.E.2    Garman, E.F.3    Papageorgiou, A.C.4    Johnson, L.N.5
  • 28
    • 0037469146 scopus 로고    scopus 로고
    • Activation loop phosphorylation and catalysis in protein kinases: Is there functional evidence for the autoinhibitor model?
    • Adams J.A. Activation loop phosphorylation and catalysis in protein kinases: is there functional evidence for the autoinhibitor model? Biochemistry. 42:2003;601-607
    • (2003) Biochemistry , vol.42 , pp. 601-607
    • Adams, J.A.1
  • 29
    • 0042424707 scopus 로고    scopus 로고
    • Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy
    • Tama F., Valle M., Frank J., Brooks C.L. III. Dynamic reorganization of the functionally active ribosome explored by normal mode analysis and cryo-electron microscopy. Proc. Natl Acad. Sci. USA. 100:2003;9319-9323
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 9319-9323
    • Tama, F.1    Valle, M.2    Frank, J.3    Brooks III, C.L.4
  • 30
    • 0034720166 scopus 로고    scopus 로고
    • Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases
    • Kawabuchi M., Satomi Y., Takao T., Shimonishi Y., Nada S., Nagai K., et al. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature. 404:2000;999-1003
    • (2000) Nature , vol.404 , pp. 999-1003
    • Kawabuchi, M.1    Satomi, Y.2    Takao, T.3    Shimonishi, Y.4    Nada, S.5    Nagai, K.6
  • 31
    • 0035800835 scopus 로고    scopus 로고
    • Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src Kinase (Csk) from lipid rafts
    • Torgersen K.M., Vang T., Abrahamsen H., Yaqub S., Horejsi V., Schraven B., et al. Release from tonic inhibition of T cell activation through transient displacement of C-terminal Src Kinase (Csk) from lipid rafts. J. Biol. Chem. 276:2001;29313-29318
    • (2001) J. Biol. Chem. , vol.276 , pp. 29313-29318
    • Torgersen, K.M.1    Vang, T.2    Abrahamsen, H.3    Yaqub, S.4    Horejsi, V.5    Schraven, B.6
  • 33
    • 0000197372 scopus 로고    scopus 로고
    • Large amplitude elastic motions in proteins from a single-parameter, atomic analysis
    • Tirion M.M. Large amplitude elastic motions in proteins from a single-parameter, atomic analysis. Phys. Rev. Letters. 77:1996;1905-1908
    • (1996) Phys. Rev. Letters , vol.77 , pp. 1905-1908
    • Tirion, M.M.1
  • 35
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • see also pp. 27-28
    • Humphrey W., Dalke A., Schulten K. VMD: visual molecular dynamics. J. Mol. Graph. 14:1996;33-38. see also pp. 27-28
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 36
    • 0028057108 scopus 로고
    • Raster3D version-2.0: A program for photorealistic molecular graphics
    • Merritt E.A., Murphy M.E.P. Raster3D version-2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D. 50:1994;869-873
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.