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.
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Ferrage, F., Dutta, K., & Cowburn, D. (2015). Identification of hydrophobic interfaces in protein-ligand complexes by selective saturation transfer NMR spectroscopy. Molecules, 20(12), 21992–21999. https://doi.org/10.3390/molecules201219824