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TitleStructure of the human PKD1-PKD2 complex.
Journal, issue, pagesScience, Vol. 361, Issue 6406, Year 2018
Publish dateSep 7, 2018
AuthorsQiang Su / Feizhuo Hu / Xiaofei Ge / Jianlin Lei / Shengqiang Yu / Tingliang Wang / Qiang Zhou / Changlin Mei / Yigong Shi /
PubMed AbstractMutations in two genes, and , account for most cases of autosomal dominant polycystic kidney disease, one of the most common monogenetic disorders. Here we report the 3.6-angstrom cryo-electron ...Mutations in two genes, and , account for most cases of autosomal dominant polycystic kidney disease, one of the most common monogenetic disorders. Here we report the 3.6-angstrom cryo-electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio. PKD1 contains a voltage-gated ion channel (VGIC) fold that interacts with PKD2 to form the domain-swapped, yet noncanonical, transient receptor potential (TRP) channel architecture. The S6 helix in PKD1 is broken in the middle, with the extracellular half, S6a, resembling pore helix 1 in a typical TRP channel. Three positively charged, cavity-facing residues on S6b may block cation permeation. In addition to the VGIC, a five-transmembrane helix domain and a cytosolic PLAT domain were resolved in PKD1. The PKD1-PKD2 complex structure establishes a framework for dissecting the function and disease mechanisms of the PKD proteins.
External linksScience / PubMed:30093605
MethodsEM (single particle)
Resolution3.2 - 3.6 Å
Structure data

6991

6a70

EMDB-6991, PDB-6a70:
Structure of the human PKD1/PKD2 complex
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-6992:
Structure of the human PKD1/PKD2 complex
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Asymmetric complex / polycystic kidney disease

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