Transferase(Phosphotransferase); domain 1
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
Three-dimensional solution structure of the src homology 2 domain of c-abl.
Secondary structure of Src homology 2 domain of c-Abl by heteronuclear NMR spectroscopy in solution.
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.
The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 57-218.
Intramolecular interactions of the regulatory domains of the Bcr-Abl kinase reveal a novel control mechanism.
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 64-121.
Crystal structure of the abl-SH3 domain complexed with a designed high-affinity peptide ligand: implications for SH3-ligand interactions.
The substrate specificity of the catalytic domain of Abl plays an important role in directing phosphorylation of the adaptor protein Crk.
Regulation of the hTERT telomerase catalytic subunit by the c-Abl tyrosine kinase.
c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines.
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 223-515.
Structural mechanism for STI-571 inhibition of abelson tyrosine kinase.
Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase.
Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).
Structure of a regulatory complex involving the Abl SH3 domain, the Crk SH2 domain, and a Crk-derived phosphopeptide.
A myristoyl/phosphotyrosine switch regulates c-Abl.
Structural basis for the autoinhibition of c-Abl tyrosine kinase.
The E.C. was transferred from 2.7.1.112 to 2.7.10.2. This enzyme is composed of the N-terminal poly-Ser region, SH3 domain, SH2 domain, protein kinase domain, nuclear localization signal region with poly-Lys, and Pro-rich domain. The PDB structure, 2abl, corresponds to the SH3 and SH2 domains, whilst the structure, 1fpu, corresponds to the kinase domain. (1opk and 1opl cover from the SH3 domain to the kinase domain.) The structures of the C-terminal domains have not been determined yet. Altough the catalytic mechanism of this enzyme has not been discussed yet, it can be similar to that of its homologous enzymes (see M00129) due to the complete conservation of active site residues.