PDBsum entry 2gjy

Cell adhesion

PDB id: 2gjy

Contents

Protein chain

144 a.a. *

* Residue conservation analysis

PDB id:

2gjy

Name:

Cell adhesion

Title:

Nmr solution structure of tensin1 ptb domain

Structure:

Tensin. Chain: a. Fragment: ptb domain. Engineered: yes

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Gene: tns. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

NMR struc:

20 models

Authors:

M.Leone,M.Pellecchia

Key ref:

M.Leone et al. (2008). The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies. Biopolymers, 89, 86-92. PubMed id: 17922498

Date:

31-Mar-06 Release date: 03-Apr-07

Protein chain

Q04205  (TENS_CHICK) -  Tensin-1 from Gallus gallus

Seq: 1744 a.a.

Struc: 144 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.1.3.- - ?????

Biopolymers 89:86-92 (2008)

PubMed id: 17922498

The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies.

M.Leone, E.C.Yu, R.C.Liddington, E.B.Pasquale, M.Pellecchia.

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.