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- W2951537592 abstract "Abstract ATP-sensitive potassium (K ATP ) channels are metabolic sensors that couple cell energetics to membrane excitability. In pancreatic β-cells, channels formed by SUR1 and Kir6.2 regulate insulin secretion and are the targets of antidiabetic sulfonylureas. Here, we used cryo-EM to elucidate structural basis of channel assembly and gating. The structure, determined in the presence of ATP and the sulfonylurea glibenclamide, at ~6Å resolution reveals a closed Kir6.2 tetrameric core with four peripheral SUR1s each anchored to a Kir6.2 by its N-terminal transmembrane domain (TMD0). Intricate interactions between TMD0, the loop following TMD0, and Kir6.2 near the proposed PIP 2 binding site, and where ATP density is observed, suggest SUR1 may contribute to ATP and PIP 2 binding to enhance Kir6.2 sensitivity to both. The SUR1-ABC core is found in an unusual inward-facing conformation whereby the two nucleotide binding domains are misaligned along a two-fold symmetry axis, revealing a possible mechanism by which glibenclamide inhibits channel activity." @default.
- W2951537592 created "2019-06-27" @default.
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- W2951537592 date "2016-12-16" @default.
- W2951537592 modified "2023-09-27" @default.
- W2951537592 title "Cryo-EM structure of the ATP-sensitive potassium channel illuminates mechanisms of assembly and gating" @default.
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- W2951537592 doi "https://doi.org/10.1101/094649" @default.
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