Structure of the human PKD1-PKD2 complex

Author:

Su Qiang1ORCID,Hu Feizhuo1ORCID,Ge Xiaofei1ORCID,Lei Jianlin2ORCID,Yu Shengqiang3,Wang Tingliang14,Zhou Qiang1,Mei Changlin3,Shi Yigong14ORCID

Affiliation:

1. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, School of Medicine, Tsinghua University, Beijing 100084, China.

2. Technology Center for Protein Sciences, Ministry of Education Key Laboratory of Protein Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

3. Department of Nephrology, Changzheng Hospital, Second Military Medical University, Shanghai 200433, China.

4. Institute of Biology, Westlake Institute for Advanced Study, Westlake University, 18 Shilongshan Road, Xihu District, Hangzhou 310064, Zhejiang Province, China.

Abstract

A complex implicated in kidney health Autosomal dominant polycystic kidney disease (ADPKD) is a common genetic disease that can lead to kidney failure. Mutations in the proteins PKD1 and PKD2 are linked to the disease, but the function of these proteins remains unclear, both in physiology and disease. PKD1 has been implicated in the sensing of chemical and mechanical force stimuli, and PKD2 is proposed to be a calcium ion channel. Su et al. show that the transmembrane regions form a PKD1-PKD2 complex assembled in a 1:3 ratio. Their high-resolution cryo–electron microscopy structure confirms that the complex adopts transient receptor potential channel architecture, with some distinctive features. Mapping disease-causing mutations onto the structure suggests that pathogenesis may come from incorrect folding or trafficking of the complex rather than from disruption of channel activity. Science , this issue p. eaat9819

Funder

National Natural Science Foundation of China

Ministry of Science and Technology of the People's Republic of China

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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