2GJY

NMR Solution Structure of Tensin1 PTB Domain

2GJY の概要

• エントリーDOI: 10.2210/pdb2gjy/pdb
• 関連するPDBエントリー: 1WVH
• NMR情報: BMRB: 6986
• 分子名称: Tensin (1 entity in total)
• 機能のキーワード: focal adhesion beta sandwich, cell adhesion
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cell junction, adherens junction: Q04205
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15669.82

構造登録者

Leone, M.,Pellecchia, M. (登録日: 2006-03-31, 公開日: 2007-04-03, 最終更新日: 2024-05-29)

主引用文献

Leone, M.,Yu, E.C.,Liddington, R.C.,Pasquale, E.B.,Pellecchia, M.
The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies.
Biopolymers, 89:86-92, 2007

PubMed Abstract: Tensin is a protein confined at those discrete and specialized regions of the plasma membrane, known as focal adhesions. It contains, at the C-terminus, a phosphotyrosine binding (PTB) domain that can interact with the cytoplasmic tail of beta-integrins and is necessary for localization of the protein to cell-matrix adhesions. Here, we present the NMR solution structure of the PTB domain of tensin1. Moreover, through NMR binding studies, we demonstrate that the PTB domain of tensin1 is able to interact with phosphatidylinositol 4, 5-diphosphate (PtIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtIns(4)P), presenting higher affinity for the diphosphorylated inositide. Chemical shift mapping studies reveal a putative PtIns(4,5)P2 binding region that is distinct from the predicted integrin beta-tail recognition site. Heteronuclear NOE experiments, recorded in absence and presence of PtIns(4,5)P2, indicate that the interaction with lipids decreases the flexibility of loop regions, predicted to be important for integrin binding, and thus, proposes a possible correlation between the two distinct binding events. Therefore, our studies suggest that capture of lipids by the PTB domain of tensin1 may play a role for the protein function at focal adhesions.

PubMed: 17922498
DOI: 10.1002/bip.20862

実験手法

SOLUTION NMR