基于 NMR 的配体-蛋白质相互作用位点的 3D 结构测定，无需蛋白质共振赋值。
NMR-Based Determination of the 3D Structure of the Ligand-Protein Interaction Site without Protein Resonance Assignment.
机构信息
ETH Zürich , Laboratory of Physical Chemistry, HCI F217, Vladimir-Prelog-Weg 2, 8093 Zürich, Switzerland.
Swiss Light Source, Paul Scherrer Institute , CH-5232 Villigen, Switzerland.
出版信息
J Am Chem Soc. 2016 Apr 6;138(13):4393-400. doi: 10.1021/jacs.5b12391. Epub 2016 Mar 23.
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 (NMR(2)). 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 NMR(2) may open a new avenue for the fast and robust determination of the interaction site of ligand-protein complexes at atomic resolution.
在 X 射线晶体学中，分子置换是建立药物相关分子的结构-活性关系的主要方法。这种方法不适用于 NMR。在这里，我们建立了一种可与之媲美的方法，称为 NMR 分子置换（NMR(2)）。该方法需要实验测量配体分子内 NOE 和配体-蛋白分子间 NOE，以及先前已知的受体结构或模型。我们的研究结果表明，NMR(2) 可能为快速、稳健地确定配体-蛋白复合物的相互作用位点提供一条新途径，达到原子分辨率。
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