6A70

Structure of the human PKD1/PKD2 complex

Summary for 6A70

• Entry DOI: 10.2210/pdb6a70/pdb
• EMDB information: 6991 6992
• Descriptor: Polycystin-2, Polycystin-1 (2 entities in total)
• Functional Keywords: asymmetric complex, polycystic kidney disease, membrane protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 326895.05

Authors

Su, Q.,Hu, F.,Ge, X.,Lei, J.,Yu, S.,Wang, T.,Zhou, Q.,Mei, C.,Shi, Y. (deposition date: 2018-06-29, release date: 2018-08-15, Last modification date: 2024-03-27)

Primary citation

Su, Q.,Hu, F.,Ge, X.,Lei, J.,Yu, S.,Wang, T.,Zhou, Q.,Mei, C.,Shi, Y.
Structure of the human PKD1-PKD2 complex.
Science, 361:-, 2018

PubMed Abstract: 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.

PubMed: 30093605
DOI: 10.1126/science.aat9819

Experimental method

ELECTRON MICROSCOPY (3.6 Å)