Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.
|Abstract||The SH2 domain of cytoplasmic tyrosine kinases can enhance catalytic activity and substrate recognition, but the molecular mechanisms by which this is achieved are poorly understood. We have solved the structure of the prototypic SH2-kinase unit of the human Fes tyrosine kinase, which appears specialized for positive signaling. In its active conformation, the SH2 domain tightly interacts with the kinase N-terminal lobe and positions the kinase al ... [truncated at 450 characters in length]|
|Author||Filippakopoulos, Panagis; Kofler, Michael; Hantschel, Oliver; et al|
|Subject||Amino Acid Sequence Crystallography, X-Ray Enzyme Activation Humans Ligands Models, Molecular Molecular Sequence Data Protein Interaction Domains and Motifs Protein Structure, Tertiary Proto-Oncogene Proteins c-abl Proto-Oncogene Proteins c-fes chemistry metabolism chemistry metabolism|