메뉴 건너뛰기




Volumn 44, Issue 39, 2005, Pages 13043-13050

Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CRYSTAL ORIENTATION; CRYSTAL STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 25444472856     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050814y     Document Type: Article
Times cited : (24)

References (46)
  • 1
    • 0027267532 scopus 로고
    • Nonreceptor tyrosine protein kinases
    • Bolen, J. B. (1993) Nonreceptor tyrosine protein kinases, Oncogene 8, 2025-2031.
    • (1993) Oncogene , vol.8 , pp. 2025-2031
    • Bolen, J.B.1
  • 2
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and functions of src
    • Brown, M. T., and Cooper, J. A. (1996) Regulation, substrates and functions of src, Biochim. Biophys. Acta 1287, 121-149.
    • (1996) Biochim. Biophys. Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.A.2
  • 3
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S. M., and Brugge, J. S. (1997) Cellular functions regulated by Src family kinases, Annu. Rev. Cell Dev. Biol. 13, 513-609.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 4
    • 0031578579 scopus 로고    scopus 로고
    • The 2.35 a crystal structure of the inactivated form of chicken Src: A dynamic molecule with multiple regulatory interactions
    • Williams, J. C., Weijland, A., Gonfloni, S., Thompson, A., Courtneidge, S. A., Superti-Furga, G., and Wierenga, R. K. (1997) The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions, J. Mol. Biol. 274, 757-775.
    • (1997) J. Mol. Biol. , vol.274 , pp. 757-775
    • Williams, J.C.1    Weijland, A.2    Gonfloni, S.3    Thompson, A.4    Courtneidge, S.A.5    Superti-Furga, G.6    Wierenga, R.K.7
  • 5
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., Harrison, S. C., and Eck, M. J. (1997) Three-dimensional structure of the tyrosine kinase c-Src, Nature 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 6
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri, F., Moarefi, I., and Kuriyan, J. (1997) Crystal structure of the Src family tyrosine kinase Hck, Nature 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 7
    • 0025303196 scopus 로고
    • Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45)
    • Mustelin, T., and Altman, A. (1990) Dephosphorylation and activation of the T cell tyrosine kinase pp56lck by the leukocyte common antigen (CD45), Oncogene 5, 809-813.
    • (1990) Oncogene , vol.5 , pp. 809-813
    • Mustelin, T.1    Altman, A.2
  • 9
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young, M. A., Gonfloni, S., Superti-Furga, G., Roux, B., and Kuriyan, J. (2001) Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation, Cell 105, 115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 10
    • 0028337397 scopus 로고
    • Structure of the regulatory domains of the Src-family tyrosine kinase Lck
    • Eck, M. J., Atwell, S. K., Shoelson, S. E., and Harrison, S. C. (1994) Structure of the regulatory domains of the Src-family tyrosine kinase Lck, Nature 368, 764-769.
    • (1994) Nature , vol.368 , pp. 764-769
    • Eck, M.J.1    Atwell, S.K.2    Shoelson, S.E.3    Harrison, S.C.4
  • 12
    • 0030699928 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: Effects of phosphopeptide binding
    • Tessari, M., Gentile, L. N., Taylor, S. J., Shalloway, D. I., Nicholson, L. K., and Vuister, G. W. (1997) Heteronuclear NMR studies of the combined Src homology domains 2 and 3 of pp60 c-Src: effects of phosphopeptide binding, Biochemistry 36, 14561-14571.
    • (1997) Biochemistry , vol.36 , pp. 14561-14571
    • Tessari, M.1    Gentile, L.N.2    Taylor, S.J.3    Shalloway, D.I.4    Nicholson, L.K.5    Vuister, G.W.6
  • 13
    • 0033543211 scopus 로고    scopus 로고
    • Direct determination of changes of interdomain orientation on ligation: Use of the orientational dependence of 15N NMR relaxation in Abl SH(32)
    • Fushman, D., Xu, R., and Cowburn, D. (1999) Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32), Biochemistry 38, 10225-10230.
    • (1999) Biochemistry , vol.38 , pp. 10225-10230
    • Fushman, D.1    Xu, R.2    Cowburn, D.3
  • 14
    • 0036652846 scopus 로고    scopus 로고
    • SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn
    • Ulmer, T. S., Werner, J. M., and Campbell, I. D. (2002) SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn, Structure 10, 901-911.
    • (2002) Structure , vol.10 , pp. 901-911
    • Ulmer, T.S.1    Werner, J.M.2    Campbell, I.D.3
  • 15
    • 3042513513 scopus 로고    scopus 로고
    • Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair from the human tyrosine kinase Lck
    • Schweimer, K., Kiessling, A., Bauer, F., Hor, S., Hoffmann, S., Rosch, P., and Sticht, H. (2003) Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair from the human tyrosine kinase Lck, J. Biomol. NMR 27, 405-406.
    • (2003) J. Biomol. NMR , vol.27 , pp. 405-406
    • Schweimer, K.1    Kiessling, A.2    Bauer, F.3    Hor, S.4    Hoffmann, S.5    Rosch, P.6    Sticht, H.7
  • 16
    • 0035692486 scopus 로고    scopus 로고
    • A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles
    • Chou, J. J., Gaemers, S., Howder, B., Louis, J. M., and Bax, A. (2001) A simple apparatus for generating stretched polyacrylamide gels, yielding uniform alignment of proteins and detergent micelles, J. Biomol. NMR 21, 377-382.
    • (2001) J. Biomol. NMR , vol.21 , pp. 377-382
    • Chou, J.J.1    Gaemers, S.2    Howder, B.3    Louis, J.M.4    Bax, A.5
  • 17
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Ruckert, M., and Otting, G. (2000) Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments, J. Am. Chem. Soc. 122, 7793-7797.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 18
    • 0024449503 scopus 로고
    • Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • Kay, L. E., Torchia, D. A., and Bax, A. (1989) Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease, Biochemistry 28, 8972-8979.
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 19
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 20
    • 0028503463 scopus 로고
    • A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium
    • Farrow, N. A., Zhang, O., Forman-Kay, J. D., and Kay, L. E. (1994) A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibrium, J. Biomol. NMR 4, 727-734.
    • (1994) J. Biomol. NMR , vol.4 , pp. 727-734
    • Farrow, N.A.1    Zhang, O.2    Forman-Kay, J.D.3    Kay, L.E.4
  • 21
    • 0001484114 scopus 로고
    • Influence of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms upon longitudinal relaation rates of N-15 in macromolecules
    • Boyd, J., Hommel, U., and Campbell, I. D. (1990) Influence Of Cross-Correlation Between Dipolar and Anisotropic Chemical Shift Relaxation Mechanisms Upon Longitudinal Relaation Rates Of N-15 in Macromolecules., Chem. Phys. Lett. 175, 477-482.
    • (1990) Chem. Phys. Lett. , vol.175 , pp. 477-482
    • Boyd, J.1    Hommel, U.2    Campbell, I.D.3
  • 22
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross-correlation between dipolar and chemical-shift anisotropy relaxation mechanism on the measurement of heteronuclear T1 and T2 values in proteins
    • Kay, L. E., Nicholson, L. K., Delaglio, F., and Bax, A. (1992) Pulse Sequences for Removal of the Effects of Cross-Correlation between Dipolar and Chemical-Shift Anisotropy Relaxation Mechanism on the Measurement of Heteronuclear T1 and T2 Values in Proteins, J. Magn. Reson. 97, 359-375.
    • (1992) J. Magn. Reson. , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4
  • 23
    • 0036365970 scopus 로고    scopus 로고
    • Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation
    • Werner, J. M., Campbell, I. D., and Downing, A. K. (2002) Shape and dynamics of a calcium-binding protein investigated by nitrogen-15 NMR relaxation, Methods Mol. Biol. 173, 285-300.
    • (2002) Methods Mol. Biol. , vol.173 , pp. 285-300
    • Werner, J.M.1    Campbell, I.D.2    Downing, A.K.3
  • 24
    • 33646719091 scopus 로고
    • Model-free approach to the investigation of nuclear magnetic resonance relaxation in macromolecules
    • Lipari, G., and Szabo, A. (1982) Model-free approach to the investigation of nuclear magnetic resonance relaxation in macromolecules, J. Am. Chem. Soc. 104, 4546-4559.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 25
    • 12044256620 scopus 로고
    • Intramolecular motions of a zinc finger DNA-binding domain from xfin characterized by proton-detected natural abundance 12C heteronuclear NMR-spectroscopy
    • Palmer, A. G., Rance, M., and Wright, P. E. (1991) Intramolecular motions of a zinc finger DNA-binding domain from xfin characterized by proton-detected natural abundance 12C heteronuclear NMR-spectroscopy, J. Am. Chem. Soc. 113, 4371-4380.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4371-4380
    • Palmer, A.G.1    Rance, M.2    Wright, P.E.3
  • 26
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G., 3rd. (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme, J. Mol. Biol. 246, 144-163.
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer III, A.G.3
  • 27
    • 0032560968 scopus 로고    scopus 로고
    • Defining the orientation of the N-15 shielding tensor using N-15 NMR relaxation data for a protein in solution
    • Boyd, J., and Redfield, C. (1998) Defining the orientation of the N-15 shielding tensor using N-15 NMR relaxation data for a protein in solution, J. Am. Chem. Soc. 120, 9692-9693.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9692-9693
    • Boyd, J.1    Redfield, C.2
  • 28
    • 33644625296 scopus 로고
    • Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion
    • Woessner, D. E. (1962) Nuclear spin relaxation in ellipsoids undergoing rotational Brownian motion, J. Chem. Phys. 37, 647-654.
    • (1962) J. Chem. Phys. , vol.37 , pp. 647-654
    • Woessner, D.E.1
  • 30
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger, M., Delaglio, F., and Bax, A. (1998) Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra, J. Magn. Reson. 131, 373-378.
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 31
    • 0034884233 scopus 로고    scopus 로고
    • A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings
    • Dosset, P., Hus, J. C., Marion, D., and Blackledge, M. (2001) A novel interactive tool for rigid-body modeling of multi-domain macromolecules using residual dipolar couplings, J. Biomol. NMR 20, 223-231.
    • (2001) J. Biomol. NMR , vol.20 , pp. 223-231
    • Dosset, P.1    Hus, J.C.2    Marion, D.3    Blackledge, M.4
  • 34
    • 0034715580 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions
    • Hartley, D. A., Amdjadi, K., Hurley, T. R., Lund, T. C., Medveczky, P. G., and Sefton, B. M. (2000) Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions, Virology 276, 339-348.
    • (2000) Virology , vol.276 , pp. 339-348
    • Hartley, D.A.1    Amdjadi, K.2    Hurley, T.R.3    Lund, T.C.4    Medveczky, P.G.5    Sefton, B.M.6
  • 37
    • 0028922835 scopus 로고
    • Determination of receptor-ligand kinetic and equilibrium binding constants using surface plasmon resonance: Application to the lck SH2 domain and phosphotyrosyl peptides
    • Morelock, M. M., Ingraham, R. H., Betageri, R., and Jakes, S. (1995) Determination of receptor-ligand kinetic and equilibrium binding constants using surface plasmon resonance: application to the lck SH2 domain and phosphotyrosyl peptides, J. Med. Chem. 38, 1309-1318.
    • (1995) J. Med. Chem. , vol.38 , pp. 1309-1318
    • Morelock, M.M.1    Ingraham, R.H.2    Betageri, R.3    Jakes, S.4
  • 38
    • 9744266665 scopus 로고    scopus 로고
    • Characterization of Lck-binding elements in the herpesviral regulatory tip protein
    • Bauer, F., Hofinger, E., Hoffmann, S., Rosch, P., Schweimer, K., and Sticht, H. (2004) Characterization of Lck-binding elements in the herpesviral regulatory Tip protein. Biochemistry 43, 14932-14939.
    • (2004) Biochemistry , vol.43 , pp. 14932-14939
    • Bauer, F.1    Hofinger, E.2    Hoffmann, S.3    Rosch, P.4    Schweimer, K.5    Sticht, H.6
  • 39
    • 0023016469 scopus 로고
    • Transformation by polyoma virus middle T antigen
    • Courtneidge, S. A. (1986) Transformation by polyoma virus middle T antigen, Cancer Surv. 5, 173-182.
    • (1986) Cancer Surv. , vol.5 , pp. 173-182
    • Courtneidge, S.A.1
  • 41
    • 0031060111 scopus 로고    scopus 로고
    • Functional interaction between the SH2 domain of Fyn and tyrosine 324 of hamster polyomavirus middle-T antigen
    • Dunant, N. M., Messerschmitt, A. S., and Ballmer-Hofer, K. (1997) Functional interaction between the SH2 domain of Fyn and tyrosine 324 of hamster polyomavirus middle-T antigen, J. Virol. 71, 199-206.
    • (1997) J. Virol. , vol.71 , pp. 199-206
    • Dunant, N.M.1    Messerschmitt, A.S.2    Ballmer-Hofer, K.3
  • 42
  • 43
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra, N., and Bax, A. (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium, Science 278, 1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 44
    • 0033145058 scopus 로고    scopus 로고
    • Order matrix analysis of residual dipolar couplings using singular value decomposition
    • Losonczi, J. A., Andrec, M., Fischer, M. F. W., and Prestegard, J. H. (1999) Order matrix analysis of residual dipolar couplings using singular value decomposition, J. Magn. Reson. 138, 334-342.
    • (1999) J. Magn. Reson. , vol.138 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.F.W.3    Prestegard, J.H.4
  • 45
    • 0032879507 scopus 로고    scopus 로고
    • Free R and complete cross-validation for dipolar coupling refinement of NMR structures
    • Clore, G. M., and Garrett, D. S. (1999) Free R and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures. J. Am. Chem. Soc. 121, 9008-9012.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 46
    • 0037307095 scopus 로고    scopus 로고
    • The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation
    • Zamoyska, R., Basson, A., Filby, A., Legname, G., Lovatt, M., and Seddon, B. (2003) The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation, Immunol. Rev. 191, 107-118.
    • (2003) Immunol. Rev. , vol.191 , pp. 107-118
    • Zamoyska, R.1    Basson, A.2    Filby, A.3    Legname, G.4    Lovatt, M.5    Seddon, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.