PDB 1K04 deposited: 2001-09-18 modified: 2011-07-13
Title Crystal Structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase
Authors Arold, S.T., Hoellerer, M.K., Noble, M.E.
Structure factors resolution 1.95 rfactor 0.243 rfree 0.27
DPI 0.59 theoretical min: 0.20
Related PDB Entries 1K05

"The localization of focal adhesion kinase (FAK) to sites of integrin clustering initiates downstream signaling. The C-terminal focal adhesion targeting (FAT) domain causes this localization by interacting with talin and paxillin. FAT also mediates signaling through Grb2 via phosphorylated Y925. We report two crystal structures of the FAT domain. Large rearrangements of the structure are indicated to allow phosphorylation of Y925 and subsequent interaction with Grb2. Sequence homology and structural compatibility suggest a FAT-like fold for the C-terminal domains of CAS, Efs/Sin, and HEF1. A structure-based alignment including these proteins and the vinculin tail domain reveals a conserved region that could play a role in focal adhesion targeting. Previously postulated ""paxillin binding subdomains"" may contribute to structural integrity rather than directly to paxillin binding."

Structure 2002 Mar; 10(3):319-327 doi:10.1016/S0969-2126(02)00717-7

Cross References
Database source Identifier Description
PubMed 12005431 STRUE6
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1K04/1 1K04 1 dimer 0 2 2 2352