PDBsum entry 2mox

Signaling protein

PDB id: 2mox

Contents

Protein chain

143 a.a.

PDB id:

2mox

Name:

Signaling protein

Title:

Solution structure of tandem sh3 domain of sorbin and sh3 domain- containing protein 1

Structure:

Sorbin and sh3 domain-containing protein 1. Chain: a. Fragment: unp residues 791-930. Synonym: ponsin, sh3 domain protein 5, sh3p12, c-cbl-associated protein, cap. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: sorbs1, kiaa0894, kiaa1296, sh3d5. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

D.Zhao,C.Wang,J.Zhang,J.Wu,Y.Shi,Z.Zhang,Q.Gong

Key ref:

D.Zhao et al. (2014). Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin. J Struct Biol, 187, 194-205. PubMed id: 24878663 DOI: 10.1016/j.jsb.2014.05.009

Date:

07-May-14 Release date: 28-May-14

Protein chain

Q9BX66  (SRBS1_HUMAN) -  Sorbin and SH3 domain-containing protein 1 from Homo sapiens

Seq: 1292 a.a.

Struc: 143 a.a.*

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

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jsb.2014.05.009

J Struct Biol 187:194-205 (2014)

PubMed id: 24878663

Structural investigation of the interaction between the tandem SH3 domains of c-Cbl-associated protein and vinculin.

D.Zhao, X.Wang, J.Peng, C.Wang, F.Li, Q.Sun, Y.Zhang, J.Zhang, G.Cai, X.Zuo, J.Wu, Y.Shi, Z.Zhang, Q.Gong.

ABSTRACT

c-Cbl-associated protein (CAP) is an important cytoskeletal adaptor protein involved in the regulation of adhesion turnover. The interaction between CAP and vinculin is critical for the recruitment of CAP to focal adhesions. The tandem SH3 domains (herein termed SH3a and SH3b) of CAP are responsible for its interaction with vinculin. However, the structural mechanism underlying the interaction between CAP and vinculin is poorly understood. In this manuscript, we report the solution structure of the tandem SH3 domains of CAP. Our NMR and ITC data indicate that the SH3a and SH3b domains of CAP simultaneously bind to a long proline-rich region of vinculin with different binding specificities. Furthermore, the crystal structures of the individual SH3a and SH3b domains complexed with their substrate peptides indicate that Q807(SH3a) and D881(SH3b) are the critical residues determining the different binding specificities of the SH3 domains. Based on the obtained structural information, a model of the SH3ab-vinculin complex was generated using MD simulation and SAXS data.