Next Article in Journal
Recent Advances in the Development and Application of Radiolabeled Kinase Inhibitors for PET Imaging
Previous Article in Journal
Eco-Friendly Synthesis of Some Thiosemicarbazones and Their Applications as Intermediates for 5-Arylazothiazole Disperse Dyes
Previous Article in Special Issue
Charting a Path to Success in Virtual Screening
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,*
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
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;
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
Show Figures

Graphical abstract

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.

Show more citation formats Show less citations formats

Article Access Map by Country/Region

Search more from Scilit
Back to TopTop