Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)

Cancer Research

Volumn 62, Issue 15, 2002, Pages 4236-4243

  Nagar, Bhushan ^a,b   Bornmann, William G ^c   Pellicena, Patricia ^a,b   Schindler, Thomas ^d   Veach, Darren R ^c   Miller, W Todd ^e   Clarkson, Bayard ^c   Kuriyan, John ^a,b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

^c MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^d ROCKEFELLER UNIVERSITY   (United States)

^e STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

6 (2,6 DICHLOROPHENYL) 8 METHYL 2 (3 METHYLTHIOANILINO) 8H PYRIDO[2,3 D]PYRIMIDIN 7 ONE; ADENOSINE TRIPHOSPHATE; BCR ABL PROTEIN; IMATINIB; ONCOPROTEIN; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL TRANSFORMATION; CHRONIC MYELOID LEUKEMIA; CRYSTAL STRUCTURE; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG STRUCTURE; GENE FUSION; INSECT; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN;

AMINO ACID SEQUENCE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; ENZYME INHIBITORS; MICE; MOLECULAR SEQUENCE DATA; PIPERAZINES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; PROTO-ONCOGENE PROTEINS C-ABL; PYRIDONES; PYRIMIDINES; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036682301     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (25)

1. Cycling, stressed-out and nervous: Cellular functions of c-Abl
2. N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl
3. SHI domain autophosphorylation of P210 BCR/ABL is required for transformation but not growth factor independence
4. Effects of a selective inhibitor of the Abl tyrosine kinase on the growth of Bcr-Abl positive cells
5. Hematologic and cytogenetic responses to imatinib mesylate in chronic myelogenous leukemia
6. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
7. The pyrido[2, 3-d]pyrimidine derivative PD180970 inhibits p210Bcr-Abl tyrosine kinase and induces apoptosis of K562 leukemic cells
8. Inhibition of Src kinases by a selective tyrosine kinase inhibitor causes mitotic arrest
9. Characterization of potent inhibitors of the Bcr-Abl and the c-Kit receptor tyrosine kinases
10. Potent and selective inhibitors of the Abl-kinase: Phenylamino-pyrimidine (PAP) derivatives
11. Biochemical and cellular effects of c-Src kinase-selective pyrido[2, 3-d]pyrimidine tyrosine kinase inhibitors
12. Processing of X-ray diffraction data collected in oscillation mode
13. AMoRe: An automated package for molecular replacement
14. Crystallography & NMR system: A new software suite for macromolecular structure determination
15. Kjeldgaard Improved methods for binding protein models in electron density maps and the location of errors in these models
16. Characterization of pp60c-src tyrosine kinase activities using a continuous assay: Autoactivation of the enzyme is an intermolecular autophosphorylation process
17. The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr
18. c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
19. Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
20. Structural basis for activation of human lymphocyte kinase Lck upon tyrosine phosphorylation
21. Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor
22. Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
23. Crystal structure of the tyrosine kinase domain of the human insulin receptor
24. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
25. SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules