5FZT

The crystal structure of R7R8 in complex with a DLC1 fragment.

5FZT の概要

• エントリーDOI: 10.2210/pdb5fzt/pdb
• 分子名称: TALIN-1, RHO GTPASE-ACTIVATING PROTEIN 7, MALONATE ION, ... (4 entities in total)
• 機能のキーワード: structural protein, talin, dlc1, focal adhesion
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE); 詳細
• 細胞内の位置: Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side : P26039; Cytoplasm: Q96QB1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35582.01

構造登録者

Zacharchenko, T.,Qian, X.,Goult, B.T.,Jethwa, D.,Almeida, T.,Ballestrem, C.,Critchley, D.R.,Lowy, D.R.,Barsukov, I.L. (登録日: 2016-03-15, 公開日: 2016-04-27, 最終更新日: 2024-01-10)

主引用文献

Zacharchenko, T.,Qian, X.,Goult, B.T.,Jethwa, D.,Almeida, T.B.,Ballestrem, C.,Critchley, D.R.,Lowy, D.R.,Barsukov, I.L.
Ld Motif Recognition by Talin: Structure of the Talin-Dlc1 Complex.
Structure, 24:1130-, 2016

PubMed Abstract: Cell migration requires coordination between integrin-mediated cell adhesion to the extracellular matrix and force applied to adhesion sites. Talin plays a key role in coupling integrin receptors to the actomyosin contractile machinery, while deleted in liver cancer 1 (DLC1) is a Rho GAP that binds talin and regulates Rho, and therefore actomyosin contractility. We show that the LD motif of DLC1 forms a helix that binds to the four-helix bundle of the talin R8 domain in a canonical triple-helix arrangement. We demonstrate that the same R8 surface interacts with the paxillin LD1 and LD2 motifs. We identify key charged residues that stabilize the R8 interactions with LD motifs and demonstrate their importance in vitro and in cells. Our results suggest a network of competitive interactions in adhesion complexes that involve LD motifs, and identify mutations that can be used to analyze the biological roles of specific protein-protein interactions in cell migration.

PubMed: 27265849
DOI: 10.1016/J.STR.2016.04.016

実験手法

X-RAY DIFFRACTION (2.1 Å)