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Issue 5, 2020
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Protein–fragment complex structures derived by NMR molecular replacement

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Abstract

Recently we have established an NMR molecular replacement method, which is capable of solving the structure of the interaction site of protein–ligand complexes in a fully automated manner. While the method was successfully applied for ligands with strong and weak binding affinities, including small molecules and peptides, its applicability on ligand fragments remains to be shown. Structures of fragment–protein complexes are more challenging for the method since fragments contain only few protons. Here we show a successful application of the NMR molecular replacement method in solving structures of complexes between three derivatives of a ligand fragment and the protein receptor PIN1. We anticipate that this approach will find a broad application in fragment-based lead discovery.

Graphical abstract: Protein–fragment complex structures derived by NMR molecular replacement

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Supplementary files

Article information


Submitted
25 Feb 2020
Accepted
23 Apr 2020
First published
27 Apr 2020

This article is Open Access

RSC Med. Chem., 2020,11, 591-596
Article type
Research Article

Protein–fragment complex structures derived by NMR molecular replacement

F. Torres, D. Ghosh, D. Strotz, C. N. Chi, B. Davis and J. Orts, RSC Med. Chem., 2020, 11, 591
DOI: 10.1039/D0MD00068J

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