1K40

crystal structure of the FAT domain of focal adhesion kinase

1K40 の概要

• エントリーDOI: 10.2210/pdb1k40/pdb
• NMR情報: BMRB: 5677
• 分子名称: adhesion kinase (2 entities in total)
• 機能のキーワード: helix bundle, transferase
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cell junction, focal adhesion: P34152
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14006.39

構造登録者

Hayashi, I.,Vuori, K.,Liddington, R.C. (登録日: 2001-10-04, 公開日: 2002-02-06, 最終更新日: 2024-02-07)

主引用文献

Hayashi, I.,Vuori, K.,Liddington, R.C.
The focal adhesion targeting (FAT) region of focal adhesion kinase is a four-helix bundle that binds paxillin
Nat.Struct.Biol., 9:101-106, 2002

PubMed Abstract: Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localizing FAK to focal adhesions. We have determined the crystal structure of FAT and show that it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not. We show by mutagenesis that paxillin binding involves two hydrophobic patches on opposite faces of the bundle and propose a model in which two LD motifs of paxillin adopt amphipathic helices that augment the hydrophobic core of FAT, creating a six-helix bundle.

PubMed: 11799401
DOI: 10.1038/nsb755

実験手法

X-RAY DIFFRACTION (2.25 Å)