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Molecules 2015, 20(12), 21992-21999;

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

New York Structural Biology Center, New York, NY 10027, USA
Department of Chemistry, École Normale Supérieure-PSL Research University, 24 rue Lhomond, 75005 Paris, France
LBM, Sorbonne Universités, UPMC Univ Paris 06, 4 place Jussieu, F-75005 Paris, France
UMR 7203 LBM, CNRS, F-75005 Paris, France
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 6 May 2015 / Revised: 17 September 2015 / Accepted: 26 November 2015 / Published: 9 December 2015
(This article belongs to the Special Issue Molecular Docking in Drug Design)
Full-Text   |   PDF [3299 KB, uploaded 9 December 2015]   |  


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

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Ferrage, F.; Dutta, K.; Cowburn, D. Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy. Molecules 2015, 20, 21992-21999.

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