1KTM

SOLUTION STRUCTURE OF FAT DOMAIN OF FOCAL ADHESION KINASE

1KTM の概要

• エントリーDOI: 10.2210/pdb1ktm/pdb
• NMR情報: BMRB: 5266,5677
• 分子名称: FOCAL ADHESION KINASE 1 (1 entity in total)
• 機能のキーワード: focal adhesion kinase, fak, focal adhension targeting domain, fat, helix bundle, transferase
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cell junction, focal adhesion: Q00944
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15545.10

構造登録者

Liu, G.,Guibao, C.,Zheng, J. (登録日: 2002-01-16, 公開日: 2003-01-16, 最終更新日: 2024-05-22)

主引用文献

Liu, G.,Guibao, C.,Zheng, J.
Structural Insight into the Mechanisms of Targeting and Signaling of Focal Adhesion Kinase
Mol.Cell.Biol., 22:2751-2760, 2002

PubMed Abstract: Focal adhesion kinase (FAK) is a nonreceptor tyrosine kinase whose focal adhesion targeting (FAT) domain interacts with other focal adhesion molecules in integrin-mediated signaling. Localization of activated FAK to focal adhesions is indispensable for its function. Here we describe a solution structure of the FAT domain bound to a peptide derived from paxillin, a FAK-binding partner. The FAT domain is composed of four helices that form a "right-turn" elongated bundle; the globular fold is mainly maintained by hydrophobic interactions. The bound peptide further stabilizes the structure. Certain signaling events such as phosphorylation and molecule interplay may induce opening of the helix bundle. Such conformational change is proposed to precede departure of FAK from focal adhesions, which starts focal adhesion turnover.

PubMed: 11909967
DOI: 10.1128/MCB.22.8.2751-2760.2002

実験手法

SOLUTION NMR