1ktm | pdb_00001ktm
|
SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE
Overview
Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal, adhesion targeting (FAT) domain interacts with other focal adhesion, molecules in integrin-mediated signaling. Localization of activated FAK to, focal adhesions is indispensable for its function. Here we describe a, solution structure of the FAT domain bound to a peptide derived from, paxillin, a FAK-binding partner. The FAT domain is composed of four, helices that form a "right-turn" elongated bundle; the globular fold is, mainly maintained by hydrophobic interactions. The bound peptide further, stabilizes the structure. Certain signaling events such as phosphorylation, and molecule interplay may induce opening of the helix bundle. Such, conformational change is proposed to precede departure of FAK from focal, adhesions, which starts focal adhesion turnover.
About this Structure
1KTM is a Single protein structure of sequence from Gallus gallus. Active as Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2 Full crystallographic information is available from OCA.
Reference
Structural insight into the mechanisms of targeting and signaling of focal adhesion kinase., Liu G, Guibao CD, Zheng J, Mol Cell Biol. 2002 Apr;22(8):2751-60. PMID:11909967
Page seeded by OCA on Tue Nov 20 19:51:48 2007
