1k05
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Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase
OverviewOverview
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.
About this StructureAbout this Structure
1K05 is a Single protein structure of sequence from Homo sapiens. 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.
ReferenceReference
The structural basis of localization and signaling by the focal adhesion targeting domain., Arold ST, Hoellerer MK, Noble ME, Structure. 2002 Mar;10(3):319-27. PMID:12005431
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