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TitleCryo-EM structure of the polycystic kidney disease-like channel PKD2L1.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 1192, Year 2018
Publish dateMar 22, 2018
AuthorsQiang Su / Feizhuo Hu / Yuxia Liu / Xiaofei Ge / Changlin Mei / Shengqiang Yu / Aiwen Shen / Qiang Zhou / Chuangye Yan / Jianlin Lei / Yanqing Zhang / Xiaodong Liu / Tingliang Wang /
PubMed AbstractPKD2L1, 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 ...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.
External linksNat Commun / PubMed:29567962 / PubMed Central
MethodsEM (single particle)
Resolution3.38 Å
Structure data

6877

5z1w

EMDB-6877, PDB-5z1w:
Cryo-EM structure of polycystic kidney disease-like channel PKD2L1
Method: EM (single particle) / Resolution: 3.38 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / channel / cryo-EM

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