2gjy

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NMR Solution Structure of Tensin1 PTB Domain

Overview

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. (c) 2007, Wiley Periodicals, Inc. Biopolymers 89: 86-92, 2008.This article was, originally published online as an accepted preprint. The "Published, Online" date corresponds to the preprint version. You can request a copy, of the preprint by emailing the Biopolymers editorial office at, biopolymers@wiley.com.

About this Structure

2GJY is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies., Leone M, Yu EC, Liddington RC, Pasquale EB, Pellecchia M, Biopolymers. 2008 Jan;89(1):86-92. PMID:17922498

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