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1OPK

Structural basis for the auto-inhibition of c-Abl tyrosine kinase

Summary for 1OPK
Entry DOI10.2210/pdb1opk/pdb
Related1OPJ 1OPK
DescriptorProto-oncogene tyrosine-protein kinase ABL1, MYRISTIC ACID, 6-(2,6-DICHLOROPHENYL)-2-{[3-(HYDROXYMETHYL)PHENYL]AMINO}-8-METHYLPYRIDO[2,3-D]PYRIMIDIN-7(8H)-ONE, ... (5 entities in total)
Functional Keywordstransferase
Biological sourceMus musculus (house mouse)
Cellular locationCytoplasm, cytoskeleton: P00520
Total number of polymer chains1
Total formula weight56936.91
Authors
Nagar, B.,Hantschel, O.,Young, M.A.,Scheffzek, K.,Veach, D.,Bornmann, W.,Clarkson, B.,Superti-Furga, G.,Kuriyan, J. (deposition date: 2003-03-06, release date: 2003-04-08, Last modification date: 2023-08-16)
Primary citationNagar, B.,Hantschel, O.,Young, M.A.,Scheffzek, K.,Veach, D.,Bornmann, W.,Clarkson, B.,Superti-Furga, G.,Kuriyan, J.
Structural basis for the autoinhibition of c-Abl tyrosine kinase
Cell(Cambridge,Mass.), 112:859-871, 2003
Cited by
PubMed Abstract: c-Abl is normally regulated by an autoinhibitory mechanism, the disruption of which leads to chronic myelogenous leukemia. The details of this mechanism have been elusive because c-Abl lacks a phosphotyrosine residue that triggers the assembly of the autoinhibited form of the closely related Src kinases by internally engaging the SH2 domain. Crystal structures of c-Abl show that the N-terminal myristoyl modification of c-Abl 1b binds to the kinase domain and induces conformational changes that allow the SH2 and SH3 domains to dock onto it. Autoinhibited c-Abl forms an assembly that is strikingly similar to that of inactive Src kinases but with specific differences that explain the differential ability of the drug STI-571/Gleevec/imatinib (STI-571) to inhibit the catalytic activity of Abl, but not that of c-Src.
PubMed: 12654251
DOI: 10.1016/S0092-8674(03)00194-6
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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