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-Structure paper
| タイトル | Structure of the human PKD1-PKD2 complex. |
|---|---|
| ジャーナル・号・ページ | Science, Vol. 361, Issue 6406, Year 2018 |
| 掲載日 | 2018年9月7日 |
著者 | Qiang Su / Feizhuo Hu / Xiaofei Ge / Jianlin Lei / Shengqiang Yu / Tingliang Wang / Qiang Zhou / Changlin Mei / Yigong Shi / ![]() |
| PubMed 要旨 | 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 ...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. |
リンク | Science / PubMed:30093605 |
| 手法 | EM (単粒子) |
| 解像度 | 3.2 - 3.6 Å |
| 構造データ | ![]() EMDB-6992: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / Asymmetric complex / polycystic kidney disease |
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homo sapiens (ヒト)
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