10.1021/jacs.5b12391.s001
Julien Orts
Julien
Orts
Marielle
Aulikki Wälti
Marielle
Aulikki
Wälti
May Marsh
May
Marsh
Laura Vera
Laura
Vera
Alvar D. Gossert
Alvar D.
Gossert
Peter Güntert
Peter
Güntert
Roland Riek
Roland
Riek
NMR-Based
Determination of the 3D Structure of the
Ligand–Protein Interaction Site without Protein Resonance Assignment
American Chemical Society
2016
NMR 2
receptor structure
ligand intramolecular NOEs
Protein Resonance Assignment Molecular replacement
3 D Structure
method
interaction site
2016-03-04 00:00:00
Dataset
https://acs.figshare.com/articles/dataset/NMR_Based_Determination_of_the_3D_Structure_of_the_Ligand_Protein_Interaction_Site_without_Protein_Resonance_Assignment/3122401
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
(<i>N</i>MR<sup>2</sup>). 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 <i>N</i>MR<sup>2</sup> may open
a new avenue for the fast and robust determination of the interaction
site of ligand–protein complexes at atomic resolution.