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• W2173669563 abstract "Inositol-1,4,5-trisphosphate receptors (InsP3Rs) are ubiquitous ion channels responsible for cytosolic Ca(2+) signalling and essential for a broad array of cellular processes ranging from contraction to secretion, and from proliferation to cell death. Despite decades of research on InsP3Rs, a mechanistic understanding of their structure-function relationship is lacking. Here we present the first, to our knowledge, near-atomic (4.7 Å) resolution electron cryomicroscopy structure of the tetrameric mammalian type 1 InsP3R channel in its apo-state. At this resolution, we are able to trace unambiguously ∼85% of the protein backbone, allowing us to identify the structural elements involved in gating and modulation of this 1.3-megadalton channel. Although the central Ca(2+)-conduction pathway is similar to other ion channels, including the closely related ryanodine receptor, the cytosolic carboxy termini are uniquely arranged in a left-handed α-helical bundle, directly interacting with the amino-terminal domains of adjacent subunits. This configuration suggests a molecular mechanism for allosteric regulation of channel gating by intracellular signals." @default.
• W2173669563 created "2016-06-24" @default.
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• W2173669563 date "2015-10-12" @default.
• W2173669563 modified "2023-10-06" @default.
• W2173669563 title "Gating machinery of InsP3R channels revealed by electron cryomicroscopy" @default.
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• W2173669563 doi "https://doi.org/10.1038/nature15249" @default.
• W2173669563 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4804758" @default.
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