Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1 View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2018-12

AUTHORS

Qiang Su, Feizhuo Hu, Yuxia Liu, Xiaofei Ge, Changlin Mei, Shengqiang Yu, Aiwen Shen, Qiang Zhou, Chuangye Yan, Jianlin Lei, Yanqing Zhang, Xiaodong Liu, Tingliang Wang

ABSTRACT

PKD2L1, also termed TRPP3 from the TRPP subfamily (polycystic TRP channels), is involved in the sour sensation and other pH-dependent processes. PKD2L1 is believed to be a nonselective cation channel that can be regulated by voltage, protons, and calcium. Despite its considerable importance, the molecular mechanisms underlying PKD2L1 regulations are largely unknown. Here, we determine the PKD2L1 atomic structure at 3.38 Å resolution by cryo-electron microscopy, whereby side chains of nearly all residues are assigned. Unlike its ortholog PKD2, the pore helix (PH) and transmembrane segment 6 (S6) of PKD2L1, which are involved in upper and lower-gate opening, adopt an open conformation. Structural comparisons of PKD2L1 with a PKD2-based homologous model indicate that the pore domain dilation is coupled to conformational changes of voltage-sensing domains (VSDs) via a series of π-π interactions, suggesting a potential PKD2L1 gating mechanism. More... »

PAGES

1192

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-018-03606-0

    DOI

    http://dx.doi.org/10.1038/s41467-018-03606-0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1101677859

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/29567962


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