Journal
NATURE
Volume 527, Issue 7576, Pages 64-69Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature15247
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Funding
- Ministry of Science and Technology [2012CB911101, 2011CB910502, 2015CB910102, 2013CB910404]
- National Natural Science Foundation of China [21532004, 31570733, 31030020, 31170679, 31422016, 31422027]
- Ministry of Education
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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 Piezol (Piezol) at a resolution of 4.8 angstrom. Piezol 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 Piezol may use its peripheral regions as force sensors to gate the central ion-conducting pore.
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