Structural biology of endogenous membrane protein assemblies in native nanodiscs
Structural biology of endogenous membrane protein assemblies in native nanodiscs
复制标题
DOI：
10.1016/j.sbi.2021.03.008
复制
发表时间：
2021-08-01
影响因子：
6.8
通讯作者：
Overduin, Michael
中科院分区：
文献类型：
--
作者：
Brown, Chanelle J.;Trieber, Catharine;Overduin, Michael
两亲共聚物的出现使整体膜蛋白能够溶解到稳定的10-30 nm天然纳米圆盘中，以解决它们的多亚基结构、翻译后修饰、内源性脂质双分子层和小分子配体。这一突破定位了生物膜：蛋白质组件（memteins）作为细胞膜的基本功能单位。本文通过低温电子显微镜（cryo-EM）、透射电子显微镜、核磁共振波谱、电子顺磁共振、x射线衍射、表面等离子体共振和质谱分析，综述了天然纳米圆盘中跨膜蛋白的共聚物设计策略和表征方法。
The advent of amphiphilic copolymers enables integral membrane proteins to be solubilized into stable 10-30 nm native nanodiscs to resolve their multisubunit structures, post-translational modifications, endogenous lipid bilayers, and small molecule ligands. This breakthrough has positioned biological membrane:protein assemblies (memteins) as fundamental functional units of cellular membranes. Herein, we review copolymer design strategies and methods for the characterization of transmembrane proteins within native nanodiscs by cryo-electron microscopy (cryo-EM), transmission electron microscopy, nuclear magnetic resonance spectroscopy, electron paramagnetic resonance, X-ray diffraction, surface plasmon resonance, and mass spectrometry.