Ontology highlight
ABSTRACT:
SUBMITTER: Lietha D
PROVIDER: S-EPMC2077847 | biostudies-literature | 2007 Jun
REPOSITORIES: biostudies-literature
Lietha Daniel D Cai Xinming X Ceccarelli Derek F J DF Li Yiqun Y Schaller Michael D MD Eck Michael J MJ
Cell 20070601 6
Appropriate tyrosine kinase signaling depends on coordinated sequential coupling of protein-protein interactions with catalytic activation. Focal adhesion kinase (FAK) integrates signals from integrin and growth factor receptors to regulate cellular responses including cell adhesion, migration, and survival. Here, we describe crystal structures representing both autoinhibited and active states of FAK. The inactive structure reveals a mechanism of inhibition in which the N-terminal FERM domain di ...[more]