5Z1W

Cryo-EM structure of polycystic kidney disease-like channel PKD2L1

5Z1W の概要

• エントリーDOI: 10.2210/pdb5z1w/pdb
• EMDBエントリー: 6877
• 分子名称: Polycystic kidney disease 2-like 1 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: channel, cryo-em, membrane protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 265058.03

構造登録者

Zhang, Y.Q. (登録日: 2017-12-28, 公開日: 2018-03-28, 最終更新日: 2025-07-02)

主引用文献

Su, Q.,Hu, F.,Liu, Y.,Ge, X.,Mei, C.,Yu, S.,Shen, A.,Zhou, Q.,Yan, C.,Lei, J.,Zhang, Y.,Liu, X.,Wang, T.
Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1.
Nat Commun, 9:1192-1192, 2018

PubMed 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.

PubMed: 29567962
DOI: 10.1038/s41467-018-03606-0

実験手法

ELECTRON MICROSCOPY (3.38 Å)