1ST6

Crystal structure of a cytoskeletal protein

1ST6 の概要

• エントリーDOI: 10.2210/pdb1st6/pdb
• 分子名称: Vinculin (1 entity in total)
• 機能のキーワード: up-down bundles, cell adhesion
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cytoplasm, cytoskeleton: P12003
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 117509.47

構造登録者

Bakolitsa, C.,Liddington, R.C. (登録日: 2004-03-25, 公開日: 2004-08-03, 最終更新日: 2024-02-14)

主引用文献

Bakolitsa, C.,Cohen, D.M.,Bankston, L.A.,Bobkov, A.A.,Cadwell, G.W.,Jennings, L.,Critchley, D.R.,Craig, S.W.,Liddington, R.C.
Structural basis for vinculin activation at sites of cell adhesion.
Nature, 430:583-586, 2004

PubMed Abstract: Vinculin is a highly conserved intracellular protein with a crucial role in the maintenance and regulation of cell adhesion and migration. In the cytosol, vinculin adopts a default autoinhibited conformation. On recruitment to cell-cell and cell-matrix adherens-type junctions, vinculin becomes activated and mediates various protein-protein interactions that regulate the links between F-actin and the cadherin and integrin families of cell-adhesion molecules. Here we describe the crystal structure of the full-length vinculin molecule (1,066 amino acids), which shows a five-domain autoinhibited conformation in which the carboxy-terminal tail domain is held pincer-like by the vinculin head, and ligand binding is regulated both sterically and allosterically. We show that conformational changes in the head, tail and proline-rich domains are linked structurally and thermodynamically, and propose a combinatorial pathway to activation that ensures that vinculin is activated only at sites of cell adhesion when two or more of its binding partners are brought into apposition.

PubMed: 15195105
DOI: 10.1038/nature02610

実験手法

X-RAY DIFFRACTION (3.1 Å)