c-Abl Tyrosine Kinase Adopts Multiple Active Conformational States in Solution.

Abstract excerpt

Protein tyrosine kinases of the Abl family have diverse roles in normal cellular regulation and drive several forms of leukemia as oncogenic fusion proteins. In the crystal structure of the inactive c-Abl kinase core, the SH2 and SH3 domains dock onto the back of the kinase domain, resulting in a compact, assembled state. This inactive conformation is stabilized by the interaction of the myristoylated N-cap with...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Binding Sites
• Share to Crystallography, X-Ray