期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 53, 期 15, 页码 3840-3843出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201308389
关键词
compensatory entropy; intrinsically disordered proteins; NMR spectroscopy; osteopontin; protein complexes
资金
- Humboldt Foundation
- Gutenberg Academy of the University of Mainz
- FWF [W-1221-B03]
Intrinsically disordered proteins (IDPs) play crucial roles in protein interaction networks and in this context frequently constitute important hubs and interfaces. Here we show by a combination of NMR and EPR spectroscopy that the binding of the cytokine osteopontin (OPN) to its natural ligand, heparin, is accompanied by thermodynamically compensating structural adaptations. The core segment of OPN expands upon binding. This unfolding-upon-binding is governed primarily through electrostatic interactions between heparin and charged patches along the protein backbone and compensates for entropic penalties due to heparin-OPN binding. It is shown how structural unfolding compensates for entropic losses through ligand binding in IDPs and elucidates the interplay between structure and thermodynamics of rapid substrate-binding and -release events in IDP interaction networks.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据