Summary
PDB 1OW6 deposited: 2003-03-28 modified: 2009-02-24
Title Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase
Authors Arold, S.T., Campbell, I.D., Hoellerer, M.K., Labesse, G., Noble, M.E.M., Werner, J.M.
Method X-RAY DIFFRACTION
Structure factors resolution None rfactor None rfree None
DPI
Related PDB Entries 1OW7 1OW8
Citations

Focal adhesions (FAs) are large submembrane signaling complexes formed at sites of cellular attachment to the extracellular matrix. The interaction of LD motifs with their targets plays an important role in the assembly of FAs. We have determined the molecular basis for the recognition of two paxillin LD motifs by the FA targeting (FAT) domain of FA kinase using a combination of X-ray crystallography, solution NMR, and homology modeling. The four-helix FAT domain displays two LD binding sites on opposite sites of the molecule that bind LD peptides in a helical conformation. Threading studies suggest that the LD-interacting domain of p95PKL shares a common four-helical core with the FAT domain and the tail of vinculin, defining a structural family of LD motif binding modules.

Structure 2003 Oct; 11(10):1207-1217 doi:10.1016/j.str.2003.08.010

Cross References
Database source Identifier Description
PubMed 14527389 STRUE6
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1OW6/1 1OW6 1 pentamer 0 5 0 3251