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1SJ8

Solution Structure of the R1R2 Domains of Talin

1SJ8 の概要
エントリーDOI10.2210/pdb1sj8/pdb
関連するPDBエントリー1SJ7
分子名称Talin 1 (2 entities in total)
機能のキーワードstructural protein
由来する生物種Mus musculus (house mouse)
細胞内の位置Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By similarity): P26039
タンパク質・核酸の鎖数1
化学式量合計31512.32
構造登録者
Papagrigoriou, E.,Gingras, A.R.,Barsukov, I.L.,Critchley, D.R.,Emsley, J. (登録日: 2004-03-03, 公開日: 2004-08-24, 最終更新日: 2023-08-23)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 1sj8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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