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- W4281486598 abstract "ABSTRACT TMEM16F is a Ca 2+ -activated phospholipid scramblase in the TMEM16 family of membrane proteins. Unlike other TMEM16s exhibiting a membrane-exposed hydrophilic groove that serves as a translocation pathway for lipids, the experimentally determined structures of TMEM16F shows the groove in a closed conformation even under conditions of maximal scramblase activity. Here we describe the analysis of ∼400 µs all-atom ensemble molecular dynamics (MD) simulations of the TMEM16F dimer that revealed an allosteric mechanism leading to an open-groove state of the protein that is competent for lipid scrambling. The grove opens into a continuous hydrophilic conduit that is highly similar in structure to that seen in other activated scramblases. The allosteric pathway connects this opening to an observed destabilization of the Ca 2+ ion bound at the distal site near the dimer interface, to the dynamics of specific protein regions that produces the open-groove state seen in our MD simulations to scramble phospholipids." @default.
- W4281486598 created "2022-05-26" @default.
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- W4281486598 date "2022-05-24" @default.
- W4281486598 modified "2023-10-14" @default.
- W4281486598 title "The allosteric mechanism leading to an open-groove lipid conductive state of the TMEM16F scramblase" @default.
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- W4281486598 doi "https://doi.org/10.1101/2022.05.23.493170" @default.
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