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PDBsum entry 2nwm

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protein links
Cell adhesion PDB id
2nwm
Jmol
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 DOI: 10.1016/j.bbrc.2007.04.029
Date:
15-Nov-06     Release date:   24-Apr-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
O60504  (VINEX_HUMAN) -  Vinexin
Seq:
Struc:
 
Seq:
Struc:
671 a.a.
59 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     cell adhesion   2 terms 

 

 
DOI no: 10.1016/j.bbrc.2007.04.029 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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21080424 P.Shi, H.Wang, Z.Xi, C.Shi, Y.Xiong, and C.Tian (2011).
Site-specific ¹⁹F NMR chemical shift and side chain relaxation analysis of a membrane protein labeled with an unnatural amino acid.
  Protein Sci, 20, 224-228.  
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