Title : Cryo-EM structure of the polycystic kidney disease-like
channel PKD2L1
Abstract :
- PKD2L1 , also termed TRPP3 from the TRPP subfamily (polycystic TRP channels ), is involved in the sour sensation and other pH-dependent processes
- PKD2L1 is believed to be a nonselective cation channel that can be regulated by voltage, protons, and calcium
- Despite its considerable importance, the molecular mechanisms underlying PKD2L1 regulations are largely unknown
- Here, we determine the PKD2L1 atomic structure at 3 .38 Å resolution by cryo-electron microscopy, whereby side chains of nearly all residues are assigned
- Unlike its ortholog PKD2 , the pore helix (PH) and transmembrane segment 6 (S6) of PKD2L1 , which are involved in upper and lower-gate opening, adopt an open conformation
- Structural comparisons of PKD2L1 with a PKD2-based homologous model indicate that the pore domain dilation is coupled to conformational changes of voltage-sensing domains (VSDs) via a series of π-π interactions, suggesting a potential PKD2L1 gating mechanism