Ontology highlight
ABSTRACT:
SUBMITTER: Yigong Shi
PROVIDER: EMPIAR-10262 | biostudies-other |
REPOSITORIES: biostudies-other
Su Qiang Q Hu Feizhuo F Ge Xiaofei X Ge Xiaofei X Lei Jianlin J Yu Shengqiang S Wang Tingliang T Zhou Qiang Q Mei Changlin C Shi Yigong Y
Science (New York, N.Y.) 20180809 6406
Mutations in two genes, <i>PKD1</i> and <i>PKD2</i>, 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 P ...[more]