Identification of hydrophobic interfaces in protein-ligand complexes by selective saturation transfer NMR spectroscopy

Fabien Ferrage, Kaushik Dutta, David Cowburn

Research output: Contribution to journalArticle

1 Scopus citations


The proper characterization of protein-ligand interfaces is essential for structural biology, with implications ranging from the fundamental understanding of biological processes to pharmacology. Nuclear magnetic resonance is a powerful technique for such studies. We propose a novel approach to the direct determination of the likely pose of a peptide ligand onto a protein partner, by using frequency-selective cross-saturation with a low stringency isotopic labeling methods. Our method illustrates a complex of the Src homology 3 domain of C-terminal Src kinase with a peptide from the proline-enriched tyrosine phosphatase.

Original languageEnglish (US)
Pages (from-to)21992-21999
Number of pages8
Issue number12
Publication statusPublished - Dec 9 2015



  • Cross-saturation
  • Interface identification
  • NMR
  • SH3 ligand

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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