메뉴 건너뛰기




Volumn 66, Issue 2, 2006, Pages 1007-1014

Structure of the kinase domain of an imatinib-resistant Abl mutant in complex with the aurora kinase inhibitor VX-680

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; AURORA A KINASE; BCR ABL PROTEIN; CYCLOPROPANECARBOXYLIC ACID [4 [4 (4 METHYL 1 PIPERAZINYL) 6 (5 METHYL 2H PYRAZOL 3 YLAMINO) 2 PYRIMIDINYLTHIO]PHENYL]AMIDE; DASATINIB; ENZYME INHIBITOR; IMATINIB; ISOLEUCINE; THREONINE;

EID: 31644438945     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-2788     Document Type: Article
Times cited : (260)

References (45)
  • 1
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • Pendergast AM. The Abl family kinases: mechanisms of regulation and signaling. Adv Cancer Res 2002;85: 51-100.
    • (2002) Adv Cancer Res , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 2
    • 0038780904 scopus 로고    scopus 로고
    • Chronic myelogenous leukemia as a paradigm of early cancer and possible curative strategies
    • Clarkson B, Strife A, Wisniewski D, Lambek CL, Liu C. Chronic myelogenous leukemia as a paradigm of early cancer and possible curative strategies. Leukemia 2003; 17:1211-62.
    • (2003) Leukemia , vol.17 , pp. 1211-1262
    • Clarkson, B.1    Strife, A.2    Wisniewski, D.3    Lambek, C.L.4    Liu, C.5
  • 3
    • 2542441665 scopus 로고    scopus 로고
    • The BCR-ABL story: Bench to bedside and back
    • Wong S, Witte ON. The BCR-ABL story: bench to bedside and back. Annu Rev Immunol 2004;22: 247-306.
    • (2004) Annu Rev Immunol , vol.22 , pp. 247-306
    • Wong, S.1    Witte, O.N.2
  • 4
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-Abl tyrosine kinases
    • Hantschel O, Superti-Furga G. Regulation of the c-Abl and Bcr-Abl tyrosine kinases. Nat Rev Mol Cell Biol 2004;5:33-44.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 5
    • 0032921194 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors in chronic myeloid leukemia
    • Sawyers CL, Druker B. Tyrosine kinase inhibitors in chronic myeloid leukemia Cancer J Sci Am 1999;5:63-9.
    • (1999) Cancer J Sci Am , vol.5 , pp. 63-69
    • Sawyers, C.L.1    Druker, B.2
  • 6
    • 15944404601 scopus 로고    scopus 로고
    • The development of imatinib as a therapeutic agent for chronic myeloid leukemia
    • Deininger M, Buchdunger E, Druker BJ. The development of imatinib as a therapeutic agent for chronic myeloid leukemia. Blood 2005;105:2640-53.
    • (2005) Blood , vol.105 , pp. 2640-2653
    • Deininger, M.1    Buchdunger, E.2    Druker, B.J.3
  • 7
    • 0035810142 scopus 로고    scopus 로고
    • Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome
    • Druker BJ, Sawyers CL, Kantarjian H, et al. Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. N Engl J Med 2001;344:1038-42.
    • (2001) N Engl J Med , vol.344 , pp. 1038-1042
    • Druker, B.J.1    Sawyers, C.L.2    Kantarjian, H.3
  • 8
    • 0033816156 scopus 로고    scopus 로고
    • Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-kit and platelet-derived growth factor receptors
    • Buchdunger E, Cioffi CL, Law N, et al. Abl protein-tyrosine kinase inhibitor STI571 inhibits in vitro signal transduction mediated by c-kit and platelet-derived growth factor receptors. J Pharmacol Exp Ther 2000; 295:139-45.
    • (2000) J Pharmacol Exp Ther , vol.295 , pp. 139-145
    • Buchdunger, E.1    Cioffi, C.L.2    Law, N.3
  • 9
    • 0037103624 scopus 로고    scopus 로고
    • Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor β
    • Apperley JF, Gardembas M, Melo JV, et al. Response to imatinib mesylate in patients with chronic myeloproliferative diseases with rearrangements of the platelet-derived growth factor receptor β. N Engl J Med 2002;347:481-7.
    • (2002) N Engl J Med , vol.347 , pp. 481-487
    • Apperley, J.F.1    Gardembas, M.2    Melo, J.V.3
  • 10
    • 0036817874 scopus 로고    scopus 로고
    • Targeting the molecular pathophysiology of gastrointestinal stromal tumors with imatinib. Mechanisms, successes, and challenges to rational drug development
    • Demetri G. Targeting the molecular pathophysiology of gastrointestinal stromal tumors with imatinib. Mechanisms, successes, and challenges to rational drug development. Hematol Oncol Clin North Am 2002;16: 1115-24.
    • (2002) Hematol Oncol Clin North Am , vol.16 , pp. 1115-1124
    • Demetri, G.1
  • 11
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M, Kuriyan J. The conformational plasticity of protein kinases. Cell 2002;109:275-82.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 12
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; controlling activity through activation segment conformation
    • Nolen B, Taylor S, Ghosh G. Regulation of protein kinases; controlling activity through activation segment conformation. Mol Cell 2004;15:661-75.
    • (2004) Mol Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 14
    • 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)
    • Nagar B, Bornmann WG, Pellicena P, et al. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and Imatinib (STI-571). Cancer Res 2002;62:4236-43.
    • (2002) Cancer Res , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3
  • 15
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B, Hantschel O, Young MA, et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 2003;112:859-71.
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1    Hantschel, O.2    Young, M.A.3
  • 16
    • 2942542387 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase
    • Mol CD, Dougan DR, Schneider TR, et al. Structural basis for the autoinhibition and STI-571 inhibition of c-Kit tyrosine kinase. J Biol Chem 2004;279:31655-63.
    • (2004) J Biol Chem , vol.279 , pp. 31655-31663
    • Mol, C.D.1    Dougan, D.R.2    Schneider, T.R.3
  • 17
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T, Sicheri F, Pico A, Gazit A, Levitzki A, Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol Cell 1999;3:639-48.
    • (1999) Mol Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 18
    • 0033001789 scopus 로고    scopus 로고
    • Crystal structures of c-Src reveal features of its autoinhibitory mechanism
    • Xu W, Doshi A, Lei M, Eck MJ, Harrison SC. Crystal structures of c-Src reveal features of its autoinhibitory mechanism. Mol Cell 1999;3:629-38.
    • (1999) Mol Cell , vol.3 , pp. 629-638
    • Xu, W.1    Doshi, A.2    Lei, M.3    Eck, M.J.4    Harrison, S.C.5
  • 19
    • 0001686739 scopus 로고    scopus 로고
    • Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia
    • Shah NP, Nicoll JM, Nagar B, et al. Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia. Cancer Cell 2002;2:117-25.
    • (2002) Cancer Cell , vol.2 , pp. 117-125
    • Shah, N.P.1    Nicoll, J.M.2    Nagar, B.3
  • 20
  • 21
    • 14744274624 scopus 로고    scopus 로고
    • Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance
    • Burgess MR, Skaggs BJ, Shah NP, Lee FY, Sawyers CL. Comparative analysis of two clinically active BCR-ABL kinase inhibitors reveals the role of conformation-specific binding in resistance. Proc Natl Acad Sci U S A 2005;102:3395-400.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3395-3400
    • Burgess, M.R.1    Skaggs, B.J.2    Shah, N.P.3    Lee, F.Y.4    Sawyers, C.L.5
  • 22
    • 1642323740 scopus 로고    scopus 로고
    • Protein kinase inhibitors: Insights into drug design from structure
    • Noble ME, Endicott JA, Johnson LN. Protein kinase inhibitors: insights into drug design from structure. Science 2004;303:1800-5.
    • (2004) Science , vol.303 , pp. 1800-1805
    • Noble, M.E.1    Endicott, J.A.2    Johnson, L.N.3
  • 23
    • 0033200390 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of Src family kinases by PP1
    • Liu Y, Bishop A, Witucki L, et al. Structural basis for selective inhibition of Src family kinases by PP1. Chem Biol 1999;6:671-8.
    • (1999) Chem Biol , vol.6 , pp. 671-678
    • Liu, Y.1    Bishop, A.2    Witucki, L.3
  • 24
    • 20844448396 scopus 로고    scopus 로고
    • A new mutation in the KIT ATP pocket causes acquired resistance to imatinib in a gastrointestinal stromal tumor patient
    • Tamborini E, Bonadiman L, Greco A, et al. A new mutation in the KIT ATP pocket causes acquired resistance to imatinib in a gastrointestinal stromal tumor patient. Gastroenterology 2004;127:294-9.
    • (2004) Gastroenterology , vol.127 , pp. 294-299
    • Tamborini, E.1    Bonadiman, L.2    Greco, A.3
  • 25
    • 20144387198 scopus 로고    scopus 로고
    • Acquired resistance to imatinib in gastrointestinal stromal tumours caused by multiple KIT mutations
    • Wardelmann E, Thomas N, Merkelbach-Bruse S, et al. Acquired resistance to imatinib in gastrointestinal stromal tumours caused by multiple KIT mutations. Lancet Oncol 2005;6:249-51.
    • (2005) Lancet Oncol , vol.6 , pp. 249-251
    • Wardelmann, E.1    Thomas, N.2    Merkelbach-Bruse, S.3
  • 26
    • 14944352767 scopus 로고    scopus 로고
    • Mechanisms of resistance to imatinib mesylate in gastrointestinal stromal tumors and activity of the PKC412 inhibitor against imatinib-resistant mutants
    • Debiec-Rychter M, Cools J, Dumez H, et al. Mechanisms of resistance to imatinib mesylate in gastrointestinal stromal tumors and activity of the PKC412 inhibitor against imatinib-resistant mutants. Gastroenterology 2005;128:270-9.
    • (2005) Gastroenterology , vol.128 , pp. 270-279
    • Debiec-Rychter, M.1    Cools, J.2    Dumez, H.3
  • 27
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W, Miller VA, Politi KA, et al. Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med 2005;2:e73.
    • (2005) PLoS Med , vol.2
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3
  • 28
    • 2342639645 scopus 로고    scopus 로고
    • VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo
    • Harrington EA, Bebbington D, Moore J, et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nat Med 2004;10:262-7.
    • (2004) Nat Med , vol.10 , pp. 262-267
    • Harrington, E.A.1    Bebbington, D.2    Moore, J.3
  • 29
    • 23344440655 scopus 로고    scopus 로고
    • Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases
    • Carter TA, Wodicka LM, Shah NP, et al. Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases. Proc Natl Acad Sci U S A 2005;102:11011-6.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11011-11016
    • Carter, T.A.1    Wodicka, L.M.2    Shah, N.P.3
  • 30
    • 28844458822 scopus 로고    scopus 로고
    • High yield bacterial expression of active c-Abl and c-Src tyrosine kinases
    • Seeliger MA, Young M, Henderson MN, et al. High yield bacterial expression of active c-Abl and c-Src tyrosine kinases. Protein Sci 2005;14:3135-9.
    • (2005) Protein Sci , vol.14 , pp. 3135-3139
    • Seeliger, M.A.1    Young, M.2    Henderson, M.N.3
  • 31
    • 0022997481 scopus 로고
    • Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene
    • Shtivelman E, Lifshitz B, Gale RP, Roe BA, Canaani E. Alternative splicing of RNAs transcribed from the human abl gene and from the bcr-abl fused gene. Cell 1986;47:277-84.
    • (1986) Cell , vol.47 , pp. 277-284
    • Shtivelman, E.1    Lifshitz, B.2    Gale, R.P.3    Roe, B.A.4    Canaani, E.5
  • 32
    • 0025024995 scopus 로고
    • Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia
    • Guan KL, Dixon JE. Protein tyrosine phosphatase activity of an essential virulence determinant in Yersinia. Science 1990;249:553-6.
    • (1990) Science , vol.249 , pp. 553-556
    • Guan, K.L.1    Dixon, J.E.2
  • 33
    • 0025972090 scopus 로고
    • Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant
    • Bliska JB, Guan KL, Dixon JE, Falkow S. Tyrosine phosphate hydrolysis of host proteins by an essential Yersinia virulence determinant. Proc Natl Acad Sci U S A 1991;88:1187-91.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 1187-1191
    • Bliska, J.B.1    Guan, K.L.2    Dixon, J.E.3    Falkow, S.4
  • 34
    • 0028973603 scopus 로고
    • Characterization of pp60c-src tyrosine kinase activities using a continuous assay: Autoactivation of the enzyme is an intermolecular autophosphorylation process
    • Barker SC, Kassel DB, Weigl D, Huang X, Luther MA, Knight WB. Characterization of pp60c-src tyrosine kinase activities using a continuous assay: autoactivation of the enzyme is an intermolecular autophosphorylation process. Biochemistry 1995;34: 14843-51.
    • (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
  • 35
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997;276:307-26.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite programs for protein crystallography
    • Collaborative Computational Project N. The CCP4 suite programs for protein crystallography. Acta Cryt 1994;D50:760-3.
    • (1994) Acta Cryt , vol.D50 , pp. 760-763
  • 38
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, Adams PD, Clore GM, et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr D Biol Crystallogr 1998;54:905-21.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 905-921
    • Brunger, A.T.1    Adams, P.D.2    Clore, G.M.3
  • 39
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr 1991;A47:110-9.
    • (1991) Acta Crystallogr , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 0032215320 scopus 로고    scopus 로고
    • Databases in protein crystallography
    • CCP4 Proceedings
    • Kleywegt GJaJ, TA. Databases in protein crystallography. Acta Cryst 1998;D54:1119-31 (CCP4 Proceedings).
    • (1998) Acta Cryst , vol.D54 , pp. 1119-1131
    • Kleywegt, G.J.A.J.1
  • 41
    • 16144364951 scopus 로고    scopus 로고
    • Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation
    • Yamaguchi H, Hendrickson WA. Structural basis for activation of the human lymphocyte kinase Lck upon tyrosine phosphorylation. Nature 1996; 384:484-9.
    • (1996) Nature , vol.384 , pp. 484-489
    • Yamaguchi, H.1    Hendrickson, W.A.2
  • 42
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur MW, Thornton JW. Influence of proline residues on protein conformation. J Mol Biol 1991; 218:397-412.
    • (1991) J Mol Biol , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.W.2
  • 43
    • 1842848073 scopus 로고    scopus 로고
    • Structures of the cancer-related Aurora-A, Fak and Epha2 protein kinases from nanovolume crystallography
    • Nowakowski J, Cronin CN, Mcree DE, et al. Structures of the cancer-related Aurora-A, Fak and Epha2 protein kinases from nanovolume crystallography. Structure (Camb) 2002;10:1659-67.
    • (2002) Structure (Camb) , vol.10 , pp. 1659-1667
    • Nowakowski, J.1    Cronin, C.N.2    Mcree, D.E.3
  • 44
    • 0037044846 scopus 로고    scopus 로고
    • Crystal structure of aurora-2, an oncogenic serine/threonine kinase
    • Cheetham GM, Knegtel RM, Coll JT, et al. Crystal structure of aurora-2, an oncogenic serine/threonine kinase. J Biol Chem 2002;277:42419-22.
    • (2002) J Biol Chem , vol.277 , pp. 42419-42422
    • Cheetham, G.M.1    Knegtel, R.M.2    Coll, J.T.3
  • 45
    • 0242330123 scopus 로고    scopus 로고
    • Structural basis of Aurora-A activation by TPX2 at the mitotic spindle
    • Bayliss R, Sardon T, Vernos I, Conti E. Structural basis of Aurora-A activation by TPX2 at the mitotic spindle. Mol Cell 2003;12:851-62.
    • (2003) Mol Cell , vol.12 , pp. 851-862
    • Bayliss, R.1    Sardon, T.2    Vernos, I.3    Conti, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.