PDBsum entry 2nwm

Cell adhesion

PDB id: 2nwm

Contents

Protein chain

59 a.a. *

* Residue conservation analysis

PDB id:

2nwm

Name:

Cell adhesion

Title:

Solution structure of the first sh3 domain of human vinexin and its interaction with the peptides from vinculin

Structure:

Vinexin. Chain: a. Fragment: sh3 domain. Synonym: sorbin and sh3 domain-containing protein 3, sh3-containing adapter molecule 1, scam-1. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: vinexin. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

J.Zhang,B.Yao,J.Wu,Y.Shi

Key ref:

J.Zhang et al. (2007). Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides. Biochem Biophys Res Commun, 357, 931-937. PubMed id: 17467669

Date:

15-Nov-06 Release date: 24-Apr-07

Protein chain

O60504  (VINEX_HUMAN) -  Vinexin from Homo sapiens

Seq: 671 a.a.

Struc: 59 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

Biochem Biophys Res Commun 357:931-937 (2007)

PubMed id: 17467669

Solution structure of the first SH3 domain of human vinexin and its interaction with vinculin peptides.

J.Zhang, X.Li, B.Yao, W.Shen, H.Sun, C.Xu, J.Wu, Y.Shi.

ABSTRACT

Solution structure of the first Src homology (SH) 3 domain of human vinexin (V_SH3_1) was determined using nuclear magnetic resonance (NMR) method and revealed that it was a canonical SH3 domain, which has a typical beta-beta-beta-beta-alpha-beta fold. Using chemical shift perturbation and surface plasmon resonance experiments, we studied the binding properties of the SH3 domain with two different peptides from vinculin hinge regions: P856 and P868. The observations illustrated slightly different affinities of the two peptides binding to V_SH3_1. The interaction between P868 and V_SH3_1 belonged to intermediate exchange with a modest binding affinity, while the interaction between P856 and V_SH3_1 had a low binding affinity. The structure and ligand-binding interface of V_SH3_1 provide a structural basis for the further functional study of this important molecule.