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- W4226267576 abstract "The Ca2+-activated TRPM5 channel plays essential roles in taste perception and insulin secretion. However, the mechanism by which Ca2+ regulates TRPM5 activity remains elusive. We report cryo-EM structures of the zebrafish TRPM5 in an apo closed state, a Ca2+-bound open state, and an antagonist-bound inhibited state. We define two novel ligand binding sites: a Ca2+ site (CaICD) in the intracellular domain and an antagonist site in the transmembrane domain (TMD). The CaICD site is unique to TRPM5 and has two roles: modulating the voltage dependence and promoting Ca2+ binding to the CaTMD site, which is conserved throughout TRPM channels." @default.
- W4226267576 created "2022-05-05" @default.
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- W4226267576 date "2022-02-01" @default.
- W4226267576 modified "2023-10-16" @default.
- W4226267576 title "Structures of the TRPM5 channel elucidate mechanisms of activation and inhibition" @default.
- W4226267576 doi "https://doi.org/10.1016/j.bpj.2021.11.2636" @default.
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