Structure of the polycystic kidney disease TRP channel Polycystin-2 (PC2) View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2017-02

AUTHORS

Mariana Grieben, Ashley C W Pike, Chitra A Shintre, Elisa Venturi, Sam El-Ajouz, Annamaria Tessitore, Leela Shrestha, Shubhashish Mukhopadhyay, Pravin Mahajan, Rod Chalk, Nicola A Burgess-Brown, Rebecca Sitsapesan, Juha T Huiskonen, Elisabeth P Carpenter

ABSTRACT

Mutations in either polycystin-1 (PC1 or PKD1) or polycystin-2 (PC2, PKD2 or TRPP1) cause autosomal-dominant polycystic kidney disease (ADPKD) through unknown mechanisms. Here we present the structure of human PC2 in a closed conformation, solved by electron cryomicroscopy at 4.2-Å resolution. The structure reveals a novel polycystin-specific 'tetragonal opening for polycystins' (TOP) domain tightly bound to the top of a classic transient receptor potential (TRP) channel structure. The TOP domain is formed from two extensions to the voltage-sensor-like domain (VSLD); it covers the channel's endoplasmic reticulum lumen or extracellular surface and encloses an upper vestibule, above the pore filter, without blocking the ion-conduction pathway. The TOP-domain fold is conserved among the polycystins, including the homologous channel-like region of PC1, and is the site of a cluster of ADPKD-associated missense variants. Extensive contacts among the TOP-domain subunits, the pore and the VSLD provide ample scope for regulation through physical and chemical stimuli. More... »

PAGES

114-122

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb.3343

    DOI

    http://dx.doi.org/10.1038/nsmb.3343

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1020502141

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/27991905


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