1T01

Vinculin complexed with the VBS1 helix from talin

1T01 の概要

• エントリーDOI: 10.2210/pdb1t01/pdb
• 関連するPDBエントリー: 1sj7 1sj8
• 分子名称: unnamed protein product, Talin 1 (3 entities in total)
• 機能のキーワード: five helix bundle, cell adhesion, structural protein
• 由来する生物種: Gallus gallus (chicken); 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton: P12003; Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30929.86

構造登録者

Papagrigoriou, E.,Gingras, A.R.,Barsukov, I.L.,Critchley, D.R.,Emsley, J. (登録日: 2004-04-07, 公開日: 2004-08-24, 最終更新日: 2024-02-14)

主引用文献

PAPAGRIGORIOU, E.,GINGRAS, A.R.,BARSUKOV, I.L.,Bate, N.,Fillingham, I.J.,Patel, B.,Frank, R.,Ziegler, W.H.,Roberts, G.C.,Critchley, D.R.,Emsley, J.
Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
Embo J., 23:2942-2951, 2004

PubMed Abstract: The interaction between the cytoskeletal proteins talin and vinculin plays a key role in integrin-mediated cell adhesion and migration. We have determined the crystal structures of two domains from the talin rod spanning residues 482-789. Talin 482-655, which contains a vinculin-binding site (VBS), folds into a five-helix bundle whereas talin 656-789 is a four-helix bundle. We show that the VBS is composed of a hydrophobic surface spanning five turns of helix 4. All the key side chains from the VBS are buried and contribute to the hydrophobic core of the talin 482-655 fold. We demonstrate that the talin 482-655 five-helix bundle represents an inactive conformation, and mutations that disrupt the hydrophobic core or deletion of helix 5 are required to induce an active conformation in which the VBS is exposed. We also report the crystal structure of the N-terminal vinculin head domain in complex with an activated form of talin. Activation of the VBS in talin and the recruitment of vinculin may support the maturation of small integrin/talin complexes into more stable adhesions.

PubMed: 15272303
DOI: 10.1038/sj.emboj.7600285

実験手法

X-RAY DIFFRACTION (2.06 Å)