1TR2

Crystal structure of human full-length vinculin (residues 1-1066)

1TR2 の概要

• エントリーDOI: 10.2210/pdb1tr2/pdb
• 関連するPDBエントリー: 1RKC 1RKE 1SYQ 1YDI
• 分子名称: VINCULIN ISOFORM 1 (2 entities in total)
• 機能のキーワード: actin-binding, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton: P18206
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 237127.50

構造登録者

Borgon, R.A.,Vonrhein, C.,Bricogne, G.,Bois, P.R.,Izard, T. (登録日: 2004-06-19, 公開日: 2005-11-15, 最終更新日: 2024-10-30)

主引用文献

Borgon, R.A.,Vonrhein, C.,Bricogne, G.,Bois, P.R.,Izard, T.
Crystal Structure of Human Vinculin
Structure, 12:1189-1197, 2004

PubMed Abstract: Alterations in the actin cytoskeleton following the formation of cell-matrix and cell-cell junctions are orchestrated by vinculin. Vinculin associates with a large number of cytoskeletal and signaling proteins, and this flexibility is thought to contribute to rapid dissociation and reassociations of adhesion complexes. Intramolecular interactions between vinculin's head (Vh) and tail (Vt) domains limit access of its binding sites for other adhesion proteins. While the crystal structures of the Vh and Vt domains are known, these domains represent less than half of the entire protein and are separated by a large central region of unknown structure and function. Here we report the crystal structure of human full-length vinculin to 2.85 A resolution. In its resting state, vinculin is a loosely packed collection of alpha-helical bundles held together by Vh-Vt interactions. The three new well ordered alpha-helical bundle domains are similar in their structure to either Vh (Vh2 and Vh3) or to Vt (Vt2) and their loose packing provides the necessary flexibility that allows vinculin to interact with its various protein partners at sites of cell adhesion.

PubMed: 15242595
DOI: 10.1016/j.str.2004.05.00

実験手法

X-RAY DIFFRACTION (2.9 Å)