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Structure paper

TitleStructural Basis of Human KCNQ1 Modulation and Gating.
Journal, issue, pagesCell, Vol. 180, Issue 2, Page 340-347.e9, Year 2020
Publish dateJan 23, 2020
AuthorsJi Sun / Roderick MacKinnon /
PubMed AbstractKCNQ1, also known as Kv7.1, is a voltage-dependent K channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional properties are regulated in a tissue- ...KCNQ1, also known as Kv7.1, is a voltage-dependent K channel that regulates gastric acid secretion, salt and glucose homeostasis, and heart rhythm. Its functional properties are regulated in a tissue-specific manner through co-assembly with beta subunits KCNE1-5. In non-excitable cells, KCNQ1 forms a complex with KCNE3, which suppresses channel closure at negative membrane voltages that otherwise would close it. Pore opening is regulated by the signaling lipid PIP2. Using cryoelectron microscopy (cryo-EM), we show that KCNE3 tucks its single-membrane-spanning helix against KCNQ1, at a location that appears to lock the voltage sensor in its depolarized conformation. Without PIP2, the pore remains closed. Upon addition, PIP2 occupies a site on KCNQ1 within the inner membrane leaflet, which triggers a large conformational change that leads to dilation of the pore's gate. It is likely that this mechanism of PIP2 activation is conserved among Kv7 channels.
External linksCell / PubMed:31883792 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.9 Å
Structure data

20965

6uzz

EMDB-20965, PDB-6uzz:
structure of human KCNQ1-CaM complex
Method: EM (single particle) / Resolution: 3.1 Å

20966

6v00

EMDB-20966, PDB-6v00:
structure of human KCNQ1-KCNE3-CaM complex
Method: EM (single particle) / Resolution: 3.1 Å

20967

6v01

EMDB-20967, PDB-6v01:
structure of human KCNQ1-KCNE3-CaM complex with PIP2
Method: EM (single particle) / Resolution: 3.9 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PT5:
[(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho / phospholipid*YM

Source
  • homo sapiens (human)
  • anaplasma marginale (bacteria)
KeywordsMEMBRANE PROTEIN / potassium channel / KCNQ1 / CaM

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