1K05

Crystal structure of the Focal Adhesion Targeting Domain of Focal Adhesion Kinase

Summary for 1K05

• Entry DOI: 10.2210/pdb1k05/pdb
• Related: 1K04
• NMR Information: BMRB: 5677
• Descriptor: FOCAL ADHESION KINASE 1 (2 entities in total)
• Functional Keywords: up-down-up-down four helical bundle, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, focal adhesion: Q05397
• Total number of polymer chains: 3
• Total formula weight: 53849.09

Authors

Arold, S.T.,Hoellerer, M.K.,Noble, M.E.M. (deposition date: 2001-09-18, release date: 2002-01-30, Last modification date: 2024-02-07)

Primary citation

Arold, S.T.,Hoellerer, M.K.,Noble, M.E.
The structural basis of localization and signaling by the focal adhesion targeting domain.
Structure, 10:319-327, 2002

PubMed Abstract: 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.

PubMed: 12005431
DOI: 10.1016/S0969-2126(02)00717-7

Experimental method

X-RAY DIFFRACTION (2.9 Å)