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1OW8

Paxillin LD2 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase

Summary for 1OW8
Entry DOI10.2210/pdb1ow8/pdb
Related1K05
DescriptorFocal adhesion kinase 1, Paxillin (3 entities in total)
Functional Keywords4 helical bundle, amphiphatic helix, transferase
Biological sourceHomo sapiens (human)
More
Cellular locationCell junction, focal adhesion: Q05397
Total number of polymer chains5
Total formula weight56595.13
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 citationHoellerer, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

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