Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR SpectroscopyReport as inadecuate




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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



These authors contributed equally to this work.





*

Author to whom correspondence should be addressed.



Academic Editor: Derek J. McPhee

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. View Full-Text

Keywords: NMR; cross-saturation; SH3 ligand; interface identification NMR; cross-saturation; SH3 ligand; interface identification





Author: Fabien Ferrage 1,2,3,4,†, Kaushik Dutta 1,† and David Cowburn 1,5,*

Source: http://mdpi.com/



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