2018
DOI: 10.1038/s41467-018-03606-0
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Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1

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 as… Show more

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Cited by 55 publications
(87 citation statements)
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“…In the case of PC1, the detached CTF may also have NTF-independent channel function when assembled with PC2 (Fig 4). The cryo-EM structure of PC1/PC2 was solved using a truncated PC1 fragment containing the CTF lacking the intracellular C-terminal tail [44]. The structure shows that this PC1 fragment assembles with PC2 into a channel-like complex [44], consistent with our functional data.…”
Section: Discussionsupporting
confidence: 75%
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“…In the case of PC1, the detached CTF may also have NTF-independent channel function when assembled with PC2 (Fig 4). The cryo-EM structure of PC1/PC2 was solved using a truncated PC1 fragment containing the CTF lacking the intracellular C-terminal tail [44]. The structure shows that this PC1 fragment assembles with PC2 into a channel-like complex [44], consistent with our functional data.…”
Section: Discussionsupporting
confidence: 75%
“…The cryo-EM structure of PC1/PC2 was solved using a truncated PC1 fragment containing the CTF lacking the intracellular C-terminal tail [44]. The structure shows that this PC1 fragment assembles with PC2 into a channel-like complex [44], consistent with our functional data. We further show that the shorter fragment, TLD, retains channel function when associated with PC2 ( Fig 4F-H).…”
Section: Discussionsupporting
confidence: 75%
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