通过核磁共振化学位移映射展示蛋白质-蛋白质相互作用特异性
Demonstration of protein-protein interaction specificity by NMR chemical shift mapping.
作者信息
Rajagopal P, Waygood E B, Reizer J, Saier M H, Klevit R E
机构信息
University of Washington, Biomolecular Structure Center, Seattle, Washington 98195-7742, USA.
出版信息
Protein Sci. 1997 Dec;6(12):2624-7. doi: 10.1002/pro.5560061214.
Abstract
Chemical shift mapping is becoming a popular method for studying protein-protein interactions in solution. The technique is used to identify putative sites of interaction on a protein surface by detecting chemical shift perturbations in simple (1H, 15N)-HSQC NMR spectra of a uniformly labeled protein as a function of added (unlabeled) target protein. The high concentrations required for these experiments raise questions concerning the possibility for non-specific interactions being detected, thereby compromising the information obtained. We demonstrate here that the simple chemical shift mapping approach faithfully reproduces the known functional specificities among pairs of closely related proteins from the phosphoenolpyruvate:sugar phosphotransferase systems of Escherichia coli and Bacillus subtilis.
摘要
化学位移图谱正成为研究溶液中蛋白质-蛋白质相互作用的一种常用方法。该技术通过检测均匀标记蛋白质的简单（1H，15N）-HSQC NMR谱中化学位移扰动，作为添加（未标记）靶蛋白的函数，来识别蛋白质表面的假定相互作用位点。这些实验所需的高浓度引发了关于检测到非特异性相互作用的可能性的问题，从而影响所获得的信息。我们在此证明，简单的化学位移图谱方法忠实地再现了来自大肠杆菌和枯草芽孢杆菌磷酸烯醇丙酮酸：糖磷酸转移酶系统的密切相关蛋白质对之间已知的功能特异性。
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