Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 138, Issue 13, Pages 4393-4400Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b12391
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Funding
- ETH Zurich
- FEBS
- Lichtenberg program of Volkswagen Foundation
- Japan Society for Promotion of Science
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Molecular replacement in X-ray crystallography is the prime method for establishing structure-activity relationships of pharmaceutically relevant molecules. Such an approach is not available for NMR Here, we establish a comparable method, called NMR molecular replacement (NMR2). The method requires experimentally measured ligand intramolecular NOEs and ligand-protein intermolecular NOEs as well as a previously known receptor structure or model. Our findings demonstrate that NMR2 may open a new avenue for the fast and robust determination of the interaction site of ligand-protein complexes at atomic resolution.
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