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

Biochem Biophys Res Commun. 2007 Jun 15;357(4):931-7. doi: 10.1016/j.bbrc.2007.04.029. Epub 2007 Apr 17.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Amino Acid Sequence
  • Binding Sites
  • Computer Simulation
  • Humans
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Muscle Proteins
  • Protein Binding
  • Protein Conformation
  • Vinculin / chemistry*
  • Vinculin / ultrastructure*
  • src Homology Domains*

Substances

  • Adaptor Proteins, Signal Transducing
  • Muscle Proteins
  • SORBS3 protein, human
  • VCL protein, human
  • Vinculin