3G9W

Crystal Structure of Talin2 F2-F3 in Complex with the Integrin Beta1D Cytoplasmic Tail

3G9W の概要

• エントリーDOI: 10.2210/pdb3g9w/pdb
• 分子名称: Talin-2, Integrin beta-1D, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: protein-protein complex, ph domain superfold, ptb domain, helical bundle, intrinsically unstructured, cell adhesion
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Cell junction, focal adhesion (By similarity): Q71LX4; Cell membrane; Single-pass type I membrane protein. Isoform 5: Cell membrane, sarcolemma (By similarity): P05556
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64670.16

構造登録者

Anthis, N.J.,Wegener, K.L.,Ye, F.,Kim, C.,Lowe, E.D.,Vakonakis, I.,Bate, N.,Critchley, D.R.,Ginsberg, M.H.,Campbell, I.D. (登録日: 2009-02-15, 公開日: 2009-10-20, 最終更新日: 2023-11-01)

主引用文献

Anthis, N.J.,Wegener, K.L.,Ye, F.,Kim, C.,Goult, B.T.,Lowe, E.D.,Vakonakis, I.,Bate, N.,Critchley, D.R.,Ginsberg, M.H.,Campbell, I.D.
The structure of an integrin/talin complex reveals the basis of inside-out signal transduction
Embo J., 28:3623-3632, 2009

PubMed Abstract: Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the beta integrin subunit. Here, we report the first structure of talin bound to an authentic full-length beta integrin tail. Using biophysical and whole cell measurements, we show that a specific ionic interaction between the talin F3 domain and the membrane-proximal helix of the beta tail disrupts an integrin alpha/beta salt bridge that helps maintain the integrin inactive state. Second, we identify a positively charged surface on the talin F2 domain that precisely orients talin to disrupt the heterodimeric integrin transmembrane (TM) complex. These results show key structural features that explain the ability of talin to mediate inside-out TM signalling.

PubMed: 19798053
DOI: 10.1038/emboj.2009.287

実験手法

X-RAY DIFFRACTION (2.165 Å)