6FUY

Crystal structure of human full-length vinculin-T12-A974K (residues 1-1066)

「6FMM」から置き換えられました

6FUY の概要

• エントリーDOI: 10.2210/pdb6fuy/pdb
• 分子名称: Vinculin, CALCIUM ION (3 entities in total)
• 機能のキーワード: mechanosensitive self-inhibition adapter, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Peripheral membrane protein ; Cytoplasmic side : P18206
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 116699.31

構造登録者

Chorev, D.S.,Volberg, T.,Livne, A.,Eisenstein, M.,Martins, B.,Kam, Z.,Jockusch, B.M.,Medalia, O.,Sharon, M.,Geiger, B. (登録日: 2018-02-28, 公開日: 2018-03-14, 最終更新日: 2024-01-17)

主引用文献

Chorev, D.S.,Volberg, T.,Livne, A.,Eisenstein, M.,Martins, B.,Kam, Z.,Jockusch, B.M.,Medalia, O.,Sharon, M.,Geiger, B.
Conformational states during vinculin unlocking differentially regulate focal adhesion properties.
Sci Rep, 8:2693-2693, 2018

PubMed Abstract: Focal adhesions (FAs) are multi-protein complexes that connect the actin cytoskeleton to the extracellular matrix, via integrin receptors. The growth, stability and adhesive functionality of these structures are tightly regulated by mechanical stress, yet, despite the extensive characterization of the integrin adhesome, the detailed molecular mechanisms underlying FA mechanosensitivity are still unclear. Besides talin, another key candidate for regulating FA-associated mechanosensing, is vinculin, a prominent FA component, which possesses either closed ("auto-inhibited") or open ("active") conformation. A direct experimental demonstration, however, of the conformational transition between the two states is still absent. In this study, we combined multiple structural and biological approaches to probe the transition from the auto-inhibited to the active conformation, and determine its effects on FA structure and dynamics. We further show that the transition from a closed to an open conformation requires two sequential steps that can differentially regulate FA growth and stability.

PubMed: 29426917
DOI: 10.1038/s41598-018-21006-8

実験手法

X-RAY DIFFRACTION (3 Å)