1OW7

Paxillin LD4 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase

Summary for 1OW7

• Entry DOI: 10.2210/pdb1ow7/pdb
• Related: 1K05
• Descriptor: Focal adhesion kinase 1, Paxillin (3 entities in total)
• Functional Keywords: 4 helical bundle, amphiphatic helix, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Cell junction, focal adhesion: Q05397
• Total number of polymer chains: 6
• Total formula weight: 57819.44

Authors

Hoellerer, M.K.,Noble, M.E.M.,Labesse, G.,Werner, J.M.,Arold, S.T. (deposition date: 2003-03-28, release date: 2003-10-21, Last modification date: 2023-08-16)

Primary citation

Hoellerer, M.K.,Noble, M.E.M.,Labesse, G.,Werner, J.M.,Arold, S.T.
Molecular Recognition of Paxillin LD Motifs by the Focal Adhesion Targeting Domain
Structure, 11:1207-1217, 2003

PubMed Abstract: 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.

PubMed: 14527389
DOI: 10.1016/j.str.2003.08.010

Experimental method

X-RAY DIFFRACTION (2.6 Å)