Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein-peptide interactions

Chem Commun (Camb). 2010 Oct 28;46(40):7533-5. doi: 10.1039/c0cc01846e. Epub 2010 Sep 13.

Abstract

We report the first example of peptide-protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in dramatically reduced overlap, was applied to the interaction of the integrin αvβ6 with a known peptide ligand and highlights novel contact points between the substrate and target protein.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Neoplasm / chemistry
  • Antigens, Neoplasm / metabolism*
  • Binding Sites
  • Foot-and-Mouth Disease Virus / chemistry
  • Foot-and-Mouth Disease Virus / metabolism*
  • Humans
  • Integrins / chemistry
  • Integrins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Peptides / chemistry
  • Peptides / metabolism*
  • Protein Binding
  • Receptors, Virus / chemistry
  • Receptors, Virus / metabolism*

Substances

  • Antigens, Neoplasm
  • Integrins
  • Peptides
  • Receptors, Virus
  • integrin alphavbeta6