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On May 19, 2022, the research group of researcher Chen Lei from the Institute of Molecular Medicine, School of Future Technology, Peking University, Peking University-Tsinghua Life Science Joint Center, and National Center for Biomedical Imaging published a paper entitled " Structural insights into the mechanism of pancreatic pancreas " in the journal Nature Communication.
ATP-sensitive potassium channel (K ATP ) is a hetero-octameric composition consisting of an inward rectifier Kir6 (Inward-rectifier potassium channel) channel subunit and a regulatory SUR (Sulfonylurea receptor) subunit bo.
K ATP channels contain both inhibitory and activating nucleotide binding sit.
The opening of K ATP requires PI(4,5)P 2 , but the wild-type K ATP has a low affinity for PI(4,5)P 2 , so it is not suitable for structural biology studies of purified protei.
Side view of the islet K ATP channel H175K cryo-EM pre-open state structure and bottom view from the inside of the ce.
Conformational changes of the Kir2 transmembrane domain during K ATP channel openin.
Electron density shows that the inhibitory nucleotide binding site of the closed state structure has nucleotide bound, while the inhibitory nucleotide binding site of the pre-open state structure has no ligand bindi.
This study provides a structural basis for an in-depth understanding of the regulatory mechanism of nucleotides during channel openi.
Model of the working mechanism of K ATP channel activation by Mg-nucleotides and tract activato.
The study was published on BioRxiv ( https:// ) as a preprint on November 29, 202 In November 2021, Roderick MacKinnon's group at The Rockefeller University also reported the structure of the human K ATP channel in the pre-open state in the journal PNAS 5
The first author of this study is Wang Mengmeng, a doctoral student of the CLS program at the Institute of Frontier Interdisciplinary Studies, Peking University, and Chen Lei is the corresponding auth.
Nichols, CG K ATP channels as molecular sensors of cellular metaboli.
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