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Open AccessArticle

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

by Fabien Ferrage 1,2,3,4,†, Kaushik Dutta 1,† and David Cowburn 1,5,*
1
New York Structural Biology Center, New York, NY 10027, USA
2
Department of Chemistry, École Normale Supérieure-PSL Research University, 24 rue Lhomond, 75005 Paris, France
3
LBM, Sorbonne Universités, UPMC Univ Paris 06, 4 place Jussieu, F-75005 Paris, France
4
UMR 7203 LBM, CNRS, F-75005 Paris, France
5
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Academic Editor: Derek J. McPhee
Molecules 2015, 20(12), 21992-21999; https://doi.org/10.3390/molecules201219824
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)
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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MDPI and ACS Style

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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