3KMW

Crystal structure of the ILK/alpha-parvin core complex (MgATP)

3KMW の概要

• エントリーDOI: 10.2210/pdb3kmw/pdb
• 関連するPDBエントリー: 3KMU
• 分子名称: Integrin-linked kinase, Alpha-parvin, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: cell adhesion, ank repeat, atp-binding, cell junction, cell membrane, integrin-binding protein, membrane, nucleotide-binding, phosphoprotein, pseudokinase, actin-binding, alternative splicing, cytoplasm, cytoskeleton
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell junction, focal adhesion: Q13418 Q9NVD7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46346.57

構造登録者

Fukuda, K.,Qin, J. (登録日: 2009-11-11, 公開日: 2009-12-29, 最終更新日: 2023-09-06)

主引用文献

Fukuda, K.,Gupta, S.,Chen, K.,Wu, C.,Qin, J.
The pseudoactive site of ILK is essential for its binding to alpha-Parvin and localization to focal adhesions.
Mol.Cell, 36:819-830, 2009

PubMed Abstract: Integrin-linked kinase (ILK) plays a pivotal role in connecting transmembrane receptor integrin to the actin cytoskeleton and thereby regulating diverse cell-adhesion-dependent processes. The kinase domain (KD) of ILK is indispensable for its function, but the underlying molecular basis remains enigmatic. Here we present the crystal structure of the ILK KD bound to its cytoskeletal regulator, the C-terminal calponin homology domain of alpha-parvin. While maintaining a canonical kinase fold, the ILK KD displays a striking pseudoactive site conformation. We show that rather than performing the kinase function, this conformation specifically recognizes alpha-parvin for promoting effective assembly of ILK into focal adhesions. The alpha-parvin-bound ILK KD can simultaneously engage integrin beta cytoplasmic tails. These results thus define ILK as a distinct pseudokinase that mechanically couples integrin and alpha-parvin for mediating cell adhesion. They also highlight functional diversity of the kinase fold and its "active" site in mediating many biological processes.

PubMed: 20005845
DOI: 10.1016/j.molcel.2009.11.028

実験手法

X-RAY DIFFRACTION (2 Å)