3S90

Human vinculin head domain Vh1 (residues 1-252) in complex with murine talin (VBS33; residues 1512-1546)

3S90 の概要

• エントリーDOI: 10.2210/pdb3s90/pdb
• 関連するPDBエントリー: 1rkc 1syq 1t01 2bif 2x0c 3rf3
• 分子名称: Vinculin, Talin-1 (3 entities in total)
• 機能のキーワード: four-helix bundle, cell adhesion, focal adhesion
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P18206; Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side : P26039
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64738.98

構造登録者

Yogesha, S.D.,Sharff, A.,Bricogne, G.,Izard, T. (登録日: 2011-05-31, 公開日: 2011-06-22, 最終更新日: 2023-09-13)

主引用文献

Yogesha, S.D.,Sharff, A.,Bricogne, G.,Izard, T.
Intermolecular versus intramolecular interactions of the vinculin binding site 33 of talin.
Protein Sci., 20:1471-1476, 2011

PubMed Abstract: The cytoskeletal proteins talin and vinculin are localized at cell-matrix junctions and are key regulators of cell signaling, adhesion, and migration. Talin couples integrins via its FERM domain to F-actin and is an important regulator of integrin activation and clustering. The 220 kDa talin rod domain comprises several four- and five-helix bundles that harbor amphipathic α-helical vinculin binding sites (VBSs). In its inactive state, the hydrophobic VBS residues involved in binding to vinculin are buried within these helix bundles, and the mechanical force emanating from bound integrin receptors is thought necessary for their release and binding to vinculin. The crystal structure of a four-helix bundle of talin that harbors one of these VBSs, coined VBS33, was recently determined. Here we report the crystal structure of VBS33 in complex with vinculin at 2 Å resolution. Notably, comparison of the apo and vinculin bound structures shows that intermolecular interactions of the VBS33 α-helix with vinculin are more extensive than the intramolecular interactions of the VBS33 within the talin four-helix bundle.

PubMed: 21648001
DOI: 10.1002/pro.671

実験手法

X-RAY DIFFRACTION (1.97 Å)