2ABL
SH3-SH2 DOMAIN FRAGMENT OF HUMAN BCR-ABL TYROSINE KINASE
Summary for 2ABL
Entry DOI | 10.2210/pdb2abl/pdb |
Descriptor | ABL TYROSINE KINASE (2 entities in total) |
Functional Keywords | transferase, tyrosine kinase, sh3, sh2, oncoprotein |
Biological source | Homo sapiens (human) |
Cellular location | Cytoplasm, cytoskeleton. Isoform IB: Nucleus membrane; Lipid-anchor: P00519 |
Total number of polymer chains | 1 |
Total formula weight | 18122.95 |
Authors | Nam, H.-J.,Frederick, C.A. (deposition date: 1996-11-17, release date: 1997-09-04, Last modification date: 2024-04-03) |
Primary citation | Nam, H.J.,Haser, W.G.,Roberts, T.M.,Frederick, C.A. Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism. Structure, 4:1105-1114, 1996 Cited by PubMed Abstract: The Abl nonreceptor tyrosine kinase is implicated in a range of cellular processes and its transforming variants are involved in human leukemias. The N-terminal regulatory region of the Abl protein contains Src homology domains SH2 and SH3 which have been shown to be important for the regulation of its activity in vivo. These domains are often found together in the same protein and biochemical data suggest that the functions of one domain can be influenced by the other. PubMed: 8805596DOI: 10.1016/S0969-2126(96)00116-5 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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