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TitleHydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 2302, Year 2018
Publish dateJun 13, 2018
AuthorsWang Zheng / Xiaoyong Yang / Ruikun Hu / Ruiqi Cai / Laura Hofmann / Zhifei Wang / Qiaolin Hu / Xiong Liu / David Bulkley / Yong Yu / Jingfeng Tang / Veit Flockerzi / Ying Cao / Erhu Cao / Xing-Zhen Chen /
PubMed AbstractPKD2 and PKD1 genes are mutated in human autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to ...PKD2 and PKD1 genes are mutated in human autosomal dominant polycystic kidney disease. PKD2 can form either a homomeric cation channel or a heteromeric complex with the PKD1 receptor, presumed to respond to ligand(s) and/or mechanical stimuli. Here, we identify a two-residue hydrophobic gate in PKD2L1, and a single-residue hydrophobic gate in PKD2. We find that a PKD2 gain-of-function gate mutant effectively rescues PKD2 knockdown-induced phenotypes in embryonic zebrafish. The structure of a PKD2 activating mutant F604P by cryo-electron microscopy reveals a π- to α-helix transition within the pore-lining helix S6 that leads to repositioning of the gate residue and channel activation. Overall the results identify hydrophobic gates and a gating mechanism of PKD2 and PKD2L1.
External linksNat Commun / PubMed:29899465 / PubMed Central
MethodsEM (single particle)
Resolution3.54 Å
Structure data

7786

6d1w

EMDB-7786, PDB-6d1w:
human PKD2 F604P mutant
Method: EM (single particle) / Resolution: 3.54 Å

Chemicals

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

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / Ion Channel / TRP channel / PKD2 / PC2 / TRPP2

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