Equally potent inhibition of c-Src and Abl by compounds that recognize inactive kinase conformations

Cancer Research

Volumn 69, Issue 6, 2009, Pages 2384-2392

  Seeliger, Markus A ^a   Ranjitkar, Pratistha ^c   Kasap, Corynn ^d   Shan, Yibing ^e   Shaw, David E ^e   Shah, Neil P ^d   Kuriyan, John ^a,b   Maly, Dustin J ^c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF WASHINGTON   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ADENOSINE TRIPHOSPHATE; ASPARTIC ACID; BCR ABL PROTEIN; GLYCINE; IMATINIB; LEUCINE; PHENYLALANINE; PHOSPHATE; PROTEIN TYROSINE KINASE; THREONINE; CSK PROTEIN, HUMAN; ONCOPROTEIN; PIPERAZINE DERIVATIVE; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CELL GROWTH; CELL LINE; CRYSTAL STRUCTURE; DRUG POTENCY; GROWTH INHIBITION; KINETICS; MOUSE; MUTANT; MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN MOTIF; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; ENZYME ACTIVATION; HUMAN; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ANIMALS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; HUMANS; MICE; MODELS, MOLECULAR; PIPERAZINES; PROTEIN CONFORMATION; PROTEIN KINASE INHIBITORS; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE KINASES; PROTO-ONCOGENE PROTEINS; PROTO-ONCOGENE PROTEINS C-ABL; PYRIMIDINES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 65549152514     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-08-3953     Document Type: Article

References (34)

1. Sawyers CL, Hochhaus A, Feldman E, et al. Imatinib induces hematologic and cytogenetic responses in patients with chronic myelogenous leukemia in myeloid blast crisis: results of a phase II study. Blood 2002;99: 3530-39.
2. Capdeville R, Buehdunger E, Zimmermann j, Matter A. Glivec (STI571, imatinib), a rationally developed, targeted anticancer drug. Nat Rev Drug Discov 2002;1:493-502.
3. Seeliger MA, Nagar B, Frank F, et al. c~Sre binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty. Structure 2007;15:299-311.
4. 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.
5. Schindler T, Bornmann W, Pellicena P, Miller WT, Clarkson B, Kuriyan J. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 2000;2S9: 1938-42.
6. Sicheri F, Moarefi I, Kuriyan j. Crystal structure of the Src family tyrosine kinase Hck. Mature 1997;385:602-9.
7. Xu W, Harrison SC, Eck MJ. Three-dimensional structure of the tyrosine kinase c-Src. Nature 1997;385:595-602,
8. De Bondt HE, Rosenblatt J, Janearik j, et al. Crystal structure of cyelin-dependent kinase 2. Nature 1993;363: 595-602.
9. Mol CD, Dougan DR, Schneider TR, et al. Structural basis for the auto inhibition and STI-571 inhibition of c-Kit tyrosine kinase. J Biol Chem 2004;279:31655-63.
10. Levinson KM, Kuehment O, Shen K, et al. A Src-like inactive conformation in the abl tyrosine kinase domain. PLoS Biol 2006;4:el44.
11. Jacobs MD, Caron PR, Hare Bj. Classifying protein kinase structures guides use of ligand-selectivity profiles to predict inactive conformations: structure of lck/ imatinib complex. Proteins 2008;70:1451-60.
12. Shah NP, Kicoll 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.
13. Hochhaus A, La Rosee P. Imatinib therapy in chronic myelogenous leukemia: strategies to avoid and overcome resistance. Leukemia 2004;18:1321-31.
14. Soverini S, Colarossi S, Gnani A, et al. Contribution of ABL kinase domain mutations to imatinib resistance in different subsets of Philadelphia-positive patients: by the GIMEMA Working Party on Chronic Myeloid Leukemia. Clin Cancer Res 2006;12:7374-79.
15. Hochhaus A, Kreil S, Corbin AS, et al. Molecular and chromosomal mechanisms of resistance to imatinib (STI571) therapy. Leukemia 2002;16:2190-96.
16. Azam M, Seeliger MA, Gray NS, Kuriyan J, Daley GQ. Activation of tyrosine kinases by mutation of the gatekeeper threonine. Nat Struct MolBiol 2008;15:1109-18.
17. Kantarjian H, Giles F, Wunderle L, et al. Nilotinib in imatinib-resistant CML and Philadelphia chromosome-positive ALL. N Engl J Med 2006;354:2542-51.
18. Shah NP, Tran C, Lee FY, Chen P, Morris D, Sawyers CL. Overriding imatinib resistance with a novel ABL kinase inhibitor. Science 2004;305:399-401.
19. Modugno M, Casale E, Soncini C, et al. Crystal structure of the T315I Abl mutant in complex with the aurora kinases inhibitor PHA-739358. Cancer Res 2007; 67:7987-90.
20. Tamborini E, Ronadiman 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.
21. Cools j, DeAngelo DJ, Gotlib J, et al. A tyrosine kinase created by fusion of the PDGFRA and FIP1L1 genes as a therapeutic target of imatinib in idiopathic hypereosinophilic syndrome. N Engl j Med 2003;348: 1201-14.
22. Sharma SV. Bell DW, Settleman j, Haber DA. Epidermal growth factor receptor mutations in lung cancer. Nat Rev Cancer 2007;7:169-81.
23. Yun CH, Mengwasser RE, Toms AV, et al. The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP. Proc Natl Acad Sci U S A 2008;105:2070-75.
24. Seeliger MA, Young M, Henderson MN, et al. High yield bacterial expression of active e-Abl and c-Src tyrosine kinases. Protein Sci 2005;14:3135-9.
25. Shan Y, Seeliger MA, Eastwood MP, et al. A conserved protonation- dependent switch controls drug binding in the Abl kinase. Proe Natl Acad Sci U S A 2009;106:139-44.
26. McCoy Aj, Grosse-Kunstleve RW, Storoni LC, Read RJ. Likelihood-enhanced fast translation functions. Acta Crystallogr D Biol Crystallogr 2005;61:458-64.
27. Ernsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60:2126-32.
28. Murshudov GN, Vagin AA, Dodson Ej. Refinement of maerornolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53:240-55.
29. 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 USA 2005;102:3395-400.
30. Hodous BL, Geuns-Meyer SD, Hughes PE, et. al. Evolution of a highly selective and potent 2-(pyridin-2- yl)-l,3,5-triazine Tie-2 kinase inhibitor. J Med Chem 2007;50:611-26.
31. Fersht All. Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. New York: WH. Freeman; 1999. pp. xxi, 631.
32. 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.
33. Kagar B, Hantschel O, Young MA, et al. Structural basis for the autoinhibition of c-Abl tyrosine kinase. Cell 2003;112:859-71.
34. Wallace AC, Laskowski RA, Thornton JM. LIGPLOT: a program to generate schematic diagrams of protein- ligand interactions. Protein Eng 1995;8:127-34.