1OW8

Paxillin LD2 motif bound to the Focal Adhesion Targeting (FAT) domain of the Focal Adhesion Kinase

1OW8 の概要

• エントリーDOI: 10.2210/pdb1ow8/pdb
• 関連するPDBエントリー: 1K05
• 分子名称: Focal adhesion kinase 1, Paxillin (3 entities in total)
• 機能のキーワード: 4 helical bundle, amphiphatic helix, transferase
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell junction, focal adhesion: Q05397
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 56595.13

構造登録者

Hoellerer, M.K.,Noble, M.E.M.,Labesse, G.,Werner, J.M.,Arold, S.T. (登録日: 2003-03-28, 公開日: 2003-10-21, 最終更新日: 2023-08-16)

主引用文献

Hoellerer, M.K.,Noble, M.E.M.,Labesse, G.,Werner, J.M.,Arold, S.T.
Molecular Recognition of Paxillin LD Motifs by the Focal Adhesion Targeting Domain
Structure, 11:1207-1217, 2003

PubMed Abstract: Focal adhesions (FAs) are large submembrane signaling complexes formed at sites of cellular attachment to the extracellular matrix. The interaction of LD motifs with their targets plays an important role in the assembly of FAs. We have determined the molecular basis for the recognition of two paxillin LD motifs by the FA targeting (FAT) domain of FA kinase using a combination of X-ray crystallography, solution NMR, and homology modeling. The four-helix FAT domain displays two LD binding sites on opposite sites of the molecule that bind LD peptides in a helical conformation. Threading studies suggest that the LD-interacting domain of p95PKL shares a common four-helical core with the FAT domain and the tail of vinculin, defining a structural family of LD motif binding modules.

PubMed: 14527389
DOI: 10.1016/j.str.2003.08.010

実験手法

X-RAY DIFFRACTION (2.85 Å)