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

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

Author information

1
New York Structural Biology Center, New York, NY 10027, USA. fabien.ferrage@ens.fr.
2
Department of Chemistry, École Normale Supérieure-PSL Research University, 24 rue Lhomond, 75005 Paris, France. fabien.ferrage@ens.fr.
3
LBM, Sorbonne Universités, UPMC Univ Paris 06, 4 place Jussieu, F-75005 Paris, France. fabien.ferrage@ens.fr.
4
UMR 7203 LBM, CNRS, F-75005 Paris, France. fabien.ferrage@ens.fr.
5
New York Structural Biology Center, New York, NY 10027, USA. kskdutta@gmail.com.
6
New York Structural Biology Center, New York, NY 10027, USA. david.cowburn@einstein.yu.edu.
7
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, NY 10461, USA. david.cowburn@einstein.yu.edu.

Abstract

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

PMID:
26690112
DOI:
10.3390/molecules201219824
[Indexed for MEDLINE]
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