Ontology highlight
ABSTRACT:
SUBMITTER: Fukuda K
PROVIDER: S-EPMC2796127 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Fukuda Koichi K Gupta Sudhiranjan S Chen Ka K Wu Chuanyue C Qin Jun J
Molecular cell 20091201 5
Integrin-linked kinase (ILK) plays a pivotal role in connecting transmembrane receptor integrin to the actin cytoskeleton and thereby regulating diverse cell-adhesion-dependent processes. The kinase domain (KD) of ILK is indispensable for its function, but the underlying molecular basis remains enigmatic. Here we present the crystal structure of the ILK KD bound to its cytoskeletal regulator, the C-terminal calponin homology domain of alpha-parvin. While maintaining a canonical kinase fold, the ...[more]