Structural Mapping of a Chaperone- Substrate Interaction Surface**

被引：26

作者：

Callon, Morgane ^{[1
]}

Burmann, Bjoern M. ^{[1
]}

Hiller, Sebastian ^{[1
]}

机构：

[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2014年 / 53卷 / 20期

基金：

瑞士国家科学基金会; 欧洲研究理事会;

关键词：

chaperone proteins; membrane proteins; NMR spectroscopy; protein ensembles; protein-protein interactions; ESCHERICHIA-COLI; NMR CHARACTERIZATION; DENATURED STATES; PROTEIN P53; GROEL; SKP; DOMAIN; HSP90; BINDING; MODEL;

D O I：

10.1002/anie.201310963

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

NMR spectroscopy is used to detect site-specific intermolecular short-range contacts in a membrane-protein-chaperone complex. This is achieved by an orthogonal isotope-labeling scheme that permits the unambiguous detection of intermolecular NOEs between the well-folded chaperone and the unfolded substrate ensemble. The residues involved in these contacts are part of the chaperone-substrate contact interface. The approach is demonstrated for the 70kDa bacterial Skp-tOmpA complex.

引用

页码：5069 / 5072

页数：4

共 31 条

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[4]

2-B