期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 50, 页码 E3463-E3472出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1210373109
关键词
atomic force microscopy; energy landscape; intermolecular and intramolecular interactions; proteoliposomes
资金
- European Community [211800]
- Deutsche Forschungsgemeinschaft
- Lundbeck Foundation
- Lundbeck Foundation [R37-2009-3457] Funding Source: researchfish
The steroid cholesterol is an essential component of eukaryotic membranes, and it functionally modulates membrane proteins, including G protein-coupled receptors. To reveal insight into how cholesterol modulates G protein-coupled receptors, we have used dynamic single-molecule force spectroscopy to quantify the mechanical strength and flexibility, conformational variability, and kinetic and energetic stability of structural segments stabilizing the human beta(2)-adrenergic receptor (beta(2)AR) in the absence and presence of the cholesterol analog cholesteryl hemisuccinate (CHS). CHS considerably increased the kinetic, energetic, and mechanical stability of almost every structural segment at sufficient magnitude to alter the structure and functional relationship of beta(2)AR. One exception was the structural core segment of beta(2)AR, which establishes multiple ligand binding sites, and its properties were not significantly influenced by CHS.
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