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Volumn 21, Issue 6, 2006, Pages 787-798

Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; PROTEIN SH2; PROTEIN SH3; SERINE;

EID: 33644871166     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.01.035     Document Type: Article
Times cited : (190)

References (41)
  • 1
    • 0037459344 scopus 로고    scopus 로고
    • Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL
    • M. Azam, R.R. Latek, and G.Q. Daley Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL Cell 112 2003 831 843
    • (2003) Cell , vol.112 , pp. 831-843
    • Azam, M.1    Latek, R.R.2    Daley, G.Q.3
  • 2
    • 0028973603 scopus 로고
    • Characterization of pp60c-src tyrosine kinase activities using a continuous assay: Autoactivation of the enzyme is an intermolecular autophosphorylation process
    • S.C. Barker, D.B. Kassel, D. Weigl, X. Huang, M.A. Luther, and W.B. Knight Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process Biochemistry 34 1995 14843 14851
    • (1995) Biochemistry , vol.34 , pp. 14843-14851
    • Barker, S.C.1    Kassel, D.B.2    Weigl, D.3    Huang, X.4    Luther, M.A.5    Knight, W.B.6
  • 3
    • 0034634597 scopus 로고    scopus 로고
    • C-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory sites
    • B.B. Brasher, and R.A. Van Etten c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory sites J. Biol. Chem. 275 2000 35631 35637
    • (2000) J. Biol. Chem. , vol.275 , pp. 35631-35637
    • Brasher, B.B.1    Van Etten, R.A.2
  • 4
    • 0035935998 scopus 로고    scopus 로고
    • Mutational analysis of the regulatory function of the c-Abl Src homology 3 domain
    • B.B. Brasher, S. Roumiantsev, and R.A. Van Etten Mutational analysis of the regulatory function of the c-Abl Src homology 3 domain Oncogene 20 2001 7744 7752
    • (2001) Oncogene , vol.20 , pp. 7744-7752
    • Brasher, B.B.1    Roumiantsev, S.2    Van Etten, R.A.3
  • 6
    • 0038780904 scopus 로고    scopus 로고
    • Chronic myelogenous leukemia as a paradigm of early cancer and possible curative strategies
    • B. Clarkson, A. Strife, D. Wisniewski, C.L. Lambek, and C. Liu Chronic myelogenous leukemia as a paradigm of early cancer and possible curative strategies Leukemia 17 2003 1211 1262
    • (2003) Leukemia , vol.17 , pp. 1211-1262
    • Clarkson, B.1    Strife, A.2    Wisniewski, D.3    Lambek, C.L.4    Liu, C.5
  • 8
    • 20444399897 scopus 로고    scopus 로고
    • The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation
    • S.W. Cowan-Jacob, G. Fendrich, P.W. Manley, W. Jahnke, D. Fabbro, J. Liebetanz, and T. Meyer The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation Structure 13 2005 861 871
    • (2005) Structure , vol.13 , pp. 861-871
    • Cowan-Jacob, S.W.1    Fendrich, G.2    Manley, P.W.3    Jahnke, W.4    Fabbro, D.5    Liebetanz, J.6    Meyer, T.7
  • 10
    • 0028084984 scopus 로고
    • Phosphorylation of serine 985 negatively regulates the hepatocyte growth factor receptor kinase
    • L. Gandino, P. Longati, E. Medico, M. Prat, and P.M. Comoglio Phosphorylation of serine 985 negatively regulates the hepatocyte growth factor receptor kinase J. Biol. Chem. 269 1994 1815 1820
    • (1994) J. Biol. Chem. , vol.269 , pp. 1815-1820
    • Gandino, L.1    Longati, P.2    Medico, E.3    Prat, M.4    Comoglio, P.M.5
  • 13
    • 0037081093 scopus 로고    scopus 로고
    • Inhibition of the Bcr-Abl oncoprotein by Bcr requires phosphoserine 354
    • N. Hawk, T. Sun, S. Xie, Y. Wang, Y. Wu, J. Liu, and R.B. Arlinghaus Inhibition of the Bcr-Abl oncoprotein by Bcr requires phosphoserine 354 Cancer Res. 62 2002 386 390
    • (2002) Cancer Res. , vol.62 , pp. 386-390
    • Hawk, N.1    Sun, T.2    Xie, S.3    Wang, Y.4    Wu, Y.5    Liu, J.6    Arlinghaus, R.B.7
  • 14
    • 21644489425 scopus 로고    scopus 로고
    • Influence of multiple well defined conformations on small-angle scattering of proteins in solution
    • W.T. Heller Influence of multiple well defined conformations on small-angle scattering of proteins in solution Acta Crystallogr. D Biol. Crystallogr. 61 2005 33 44
    • (2005) Acta Crystallogr. D Biol. Crystallogr. , vol.61 , pp. 33-44
    • Heller, W.T.1
  • 15
    • 0021220257 scopus 로고
    • Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane
    • T. Hunter, N. Ling, and J.A. Cooper Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membrane Nature 311 1984 480 483
    • (1984) Nature , vol.311 , pp. 480-483
    • Hunter, T.1    Ling, N.2    Cooper, J.A.3
  • 17
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallogr. 34 2001 33 41
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 18
    • 0034308176 scopus 로고    scopus 로고
    • Biochemical and cellular effects of c-Src kinase-selective pyrido[2, 3-d]pyrimidine tyrosine kinase inhibitors
    • A.J. Kraker, B.G. Hartl, A.M. Amar, M.R. Barvian, H.D. Showalter, and C.W. Moore Biochemical and cellular effects of c-Src kinase-selective pyrido[2, 3-d]pyrimidine tyrosine kinase inhibitors Biochem. Pharmacol. 60 2000 885 898
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 885-898
    • Kraker, A.J.1    Hartl, B.G.2    Amar, A.M.3    Barvian, M.R.4    Showalter, H.D.5    Moore, C.W.6
  • 20
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • B.J. Mayer, H. Hirai, and R. Sakai Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases Curr. Biol. 5 1995 296 305
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 21
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and Imatinib (STI-571)
    • B. Nagar, W.G. Bornmann, P. Pellicena, T. Schindler, D.R. Veach, W.T. Miller, B. Clarkson, and J. Kuriyan Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and Imatinib (STI-571) Cancer Res. 62 2002 4236 4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 23
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • J. Navazza AMoRe: an automated package for molecular replacement Acta Crystallogr. A 50 1994 157 163
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navazza, J.1
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • A.M. Pendergast The Abl family kinases: mechanisms of regulation and signaling Adv. Cancer Res. 85 2002 51 100
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 27
    • 0025766195 scopus 로고
    • BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner
    • A.M. Pendergast, A.J. Muller, M.H. Havlik, Y. Maru, and O.N. Witte BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner Cell 66 1991 161 171
    • (1991) Cell , vol.66 , pp. 161-171
    • Pendergast, A.M.1    Muller, A.J.2    Havlik, M.H.3    Maru, Y.4    Witte, O.N.5
  • 28
  • 29
    • 0023255702 scopus 로고
    • Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units
    • F.A. Quiocho, J.S. Sack, and N.K. Vyas Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units Nature 329 1987 561 564
    • (1987) Nature , vol.329 , pp. 561-564
    • Quiocho, F.A.1    Sack, J.S.2    Vyas, N.K.3
  • 30
    • 0036463987 scopus 로고    scopus 로고
    • Disabling Abl perspectives on Abl kinase regulation and cancer therapeutics
    • C.L. Sawyers Disabling Abl perspectives on Abl kinase regulation and cancer therapeutics Cancer Cell 1 2002 13 15
    • (2002) Cancer Cell , vol.1 , pp. 13-15
    • Sawyers, C.L.1
  • 32
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src-family tyrosine kinase Hck
    • F. Sicheri, I. Moarefi, and J. Kuriyan 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
  • 33
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • D.I. Svergun Determination of the regularization parameter in indirect-transform methods using perceptual criteria J. Appl. Crystallogr. 25 1992 495 503
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 34
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D.I. Svergun, C. Barberato, and M.H. Koch CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallogr. 28 1995 768 773
    • (1995) J. Appl. Crystallogr. , vol.28 , pp. 768-773
    • Svergun, D.I.1    Barberato, C.2    Koch, M.H.3
  • 35
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 36
    • 0032937828 scopus 로고    scopus 로고
    • Cycling, stressed-out and nervous: Cellular functions of c-Abl
    • R.A. Van Etten Cycling, stressed-out and nervous: cellular functions of c-Abl Trends Cell Biol. 9 1999 179 186
    • (1999) Trends Cell Biol. , vol.9 , pp. 179-186
    • Van Etten, R.A.1
  • 37
    • 0033660312 scopus 로고    scopus 로고
    • Large-scale shape changes in proteins and macromolecular complexes
    • M.E. Wall, S.C. Gallagher, and J. Trewhella Large-scale shape changes in proteins and macromolecular complexes Annu. Rev. Phys. Chem. 51 2000 355 380
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 355-380
    • Wall, M.E.1    Gallagher, S.C.2    Trewhella, J.3
  • 38
    • 0035920195 scopus 로고    scopus 로고
    • Inhibition of c-Abl tyrosine kinase activity by filamentous actin
    • P.J. Woodring, T. Hunter, and J.Y. Wang Inhibition of c-Abl tyrosine kinase activity by filamentous actin J. Biol. Chem. 276 2001 27104 27110
    • (2001) J. Biol. Chem. , vol.276 , pp. 27104-27110
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.3
  • 39
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • W. Xu, S.C. Harrison, and M.J. Eck 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
  • 40
    • 0035313699 scopus 로고    scopus 로고
    • Phosphoserine/threonine-binding domains
    • M.B. Yaffe, and A.E. Elia Phosphoserine/threonine-binding domains Curr. Opin. Cell Biol. 13 2001 131 138
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 131-138
    • Yaffe, M.B.1    Elia, A.E.2
  • 41
    • 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
    • M.A. Young, S. Gonfloni, G. Superti-Furga, B. Roux, and J. Kuriyan Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation Cell 105 2001 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.