Identification of Hydrophobic Interfaces in Protein-Ligand Complexes by Selective Saturation Transfer NMR Spectroscopy
- Authors
- Publication Date
- Dec 09, 2015
- Identifiers
- DOI: 10.3390/molecules201219824
- OAI: oai:mdpi.com:/1420-3049/20/12/19824/
- Source
- MDPI
- Keywords
- Language
- English
- License
- Green
- External links
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.
