Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy

Molecules. 2015 Dec 9;20(12):21992-9. doi: 10.3390/molecules201219824.


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.

Keywords: NMR; SH3 ligand; cross-saturation; interface identification.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • CSK Tyrosine-Protein Kinase
  • Hydrophobic and Hydrophilic Interactions
  • Ligands
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Fragments / chemistry*
  • Protein Binding
  • Protein Tyrosine Phosphatases / chemistry
  • src Homology Domains
  • src-Family Kinases / chemistry*


  • Ligands
  • Peptide Fragments
  • CSK Tyrosine-Protein Kinase
  • src-Family Kinases
  • Protein Tyrosine Phosphatases