1OPK
Structural basis for the auto-inhibition of c-Abl tyrosine kinase
Summary for 1OPK
Entry DOI | 10.2210/pdb1opk/pdb |
Related | 1OPJ 1OPK |
Descriptor | Proto-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 Keywords | transferase |
Biological source | Mus musculus (house mouse) |
Cellular location | Cytoplasm, cytoskeleton: P00520 |
Total number of polymer chains | 1 |
Total formula weight | 56936.91 |
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 citation | Nagar, 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: 12654251DOI: 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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