机械敏感通道
压电1
离子通道
生物物理学
细胞外
跨膜结构域
跨膜蛋白
蛋白质亚单位
门控
细胞生物学
化学
生物
解剖
氨基酸
生物化学
基因
受体
作者
Jingpeng Ge,Wanqiu Li,Qiancheng Zhao,Ningning Li,Maofei Chen,Peng Zhi,Ruochong Li,Ning Gao,Bailong Xiao,Maojun Yang
出处
期刊:Nature
[Springer Nature]
日期:2015-09-21
卷期号:527 (7576): 64-69
被引量:343
摘要
Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 A. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.
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