Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6D1W

human PKD2 F604P mutant

Summary for 6D1W
Entry DOI10.2210/pdb6d1w/pdb
EMDB information7786
DescriptorPolycystin-2, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordsion channel, trp channel, pkd2, pc2, trpp2, transport protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains4
Total formula weight342639.84
Authors
Zheng, W.,Yang, X.,Bulkley, D.,Chen, X.Z.,Cao, E. (deposition date: 2018-04-12, release date: 2018-06-27, Last modification date: 2020-07-29)
Primary citationZheng, W.,Yang, X.,Hu, R.,Cai, R.,Hofmann, L.,Wang, Z.,Hu, Q.,Liu, X.,Bulkey, D.,Yu, Y.,Tang, J.,Flockerzi, V.,Cao, Y.,Cao, E.,Chen, X.Z.
Hydrophobic pore gates regulate ion permeation in polycystic kidney disease 2 and 2L1 channels.
Nat Commun, 9:2302-2302, 2018
Cited by
PubMed Abstract: 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.
PubMed: 29899465
DOI: 10.1038/s41467-018-04586-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.54 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon