Abstract
The proton-activated chloride (PAC) channel (TMEM206) was shown to be essential for proton-activated chloride currents in mammalian cells at low pHs. It plays an important role in acid-induced cell death and endosomal acidification. The conformational transition from the inactive PAC channel at neutral pH to a chloride conducting state at acidic pH was found from Cryo-EM structural data to affect several regions of the PAC trimer. The most significant conformational rearrangement involves TM1 which transitions from a parallel to a crossed conformation at pH 4.5.
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