3F6Q

Crystal structure of integrin-linked kinase ankyrin repeat domain in complex with PINCH1 LIM1 domain

3F6Q の概要

• エントリーDOI: 10.2210/pdb3f6q/pdb
• 分子名称: Integrin-linked protein kinase, LIM and senescent cell antigen-like-containing domain protein 1, IODIDE ION, ... (6 entities in total)
• 機能のキーワード: ilk, integrin-linked kinase, pinch, lim, ankyrin repeat, ank, ipp, integrin-mediated signaling, ank repeat, atp-binding, cell junction, cell membrane, kinase, membrane, nucleotide-binding, phosphoprotein, serine/threonine-protein kinase, transferase, acetylation, lim domain, metal-binding, zinc, transferase-metal binding protein complex, signaling protein-signaling protein complex, signaling protein/signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• 細胞内の位置: Cell junction, focal adhesion: Q13418 P48059
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31055.14

構造登録者

Chiswell, B.P.,Calderwood, D.A.,Boggon, T.J. (登録日: 2008-11-06, 公開日: 2008-12-02, 最終更新日: 2023-09-06)

主引用文献

Chiswell, B.P.,Zhang, R.,Murphy, J.W.,Boggon, T.J.,Calderwood, D.A.
The structural basis of integrin-linked kinase-PINCH interactions.
Proc.Natl.Acad.Sci.USA, 105:20677-20682, 2008

PubMed Abstract: The heterotrimeric complex between integrin-linked kinase (ILK), PINCH, and parvin is an essential signaling platform, serving as a convergence point for integrin and growth-factor signaling and regulating cell adhesion, spreading, and migration. We report a 1.6-A crystal structure of the ILK ankyrin repeat domain bound to the PINCH1 LIM1 domain, revealing the molecular basis of ILK-PINCH interactions and providing a structural description of this region of ILK. This structure identifies 5 ankyrin repeats in ILK, explains previous deletion mutagenesis data, permits identification of ILK and PINCH1 point mutations that disrupt the interaction, shows how zincs are coordinated by PINCH1 LIM1, and suggests that conformational flexibility and twisting between the 2 zinc fingers within the LIM1 domain may be important for ILK binding. These data provide an atomic-resolution description of a key interaction in the ILK-PINCH-parvin scaffolding complex.

PubMed: 19074270
DOI: 10.1073/pnas.0811415106

実験手法

X-RAY DIFFRACTION (1.6 Å)