1K05

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

1K05 の概要

• エントリーDOI: 10.2210/pdb1k05/pdb
• 関連するPDBエントリー: 1K04
• NMR情報: BMRB: 5677
• 分子名称: FOCAL ADHESION KINASE 1 (2 entities in total)
• 機能のキーワード: up-down-up-down four helical bundle, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell junction, focal adhesion: Q05397
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 53849.09

構造登録者

Arold, S.T.,Hoellerer, M.K.,Noble, M.E.M. (登録日: 2001-09-18, 公開日: 2002-01-30, 最終更新日: 2024-02-07)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.9 Å)