2j0m
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CRYSTAL STRUCTURE A TWO-CHAIN COMPLEX BETWEEN THE FERM AND KINASE DOMAINS OF FOCAL ADHESION KINASE.
OverviewOverview
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, directly binds the kinase domain, blocking access to the catalytic cleft, and protecting the FAK activation loop from Src phosphorylation., Additionally, the FERM domain sequesters the Tyr397 autophosphorylation, and Src recruitment site, which lies in the linker connecting the FERM and, kinase ... [(full description)]
About this StructureAbout this Structure
2J0M is a [Single protein] structure of sequence from [Gallus gallus] with 4ST as [ligand]. Active as [Non-specific protein-tyrosine kinase], with EC number [2.7.10.2]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural basis for the autoinhibition of focal adhesion kinase., Lietha D, Cai X, Ceccarelli DF, Li Y, Schaller MD, Eck MJ, Cell. 2007 Jun 15;129(6):1177-87. PMID:17574028
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