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-Structure paper
タイトル | Structural insights into the mechanism of pancreatic K channel regulation by nucleotides. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 2770, Year 2022 |
掲載日 | 2022年5月19日 |
著者 | Mengmeng Wang / Jing-Xiang Wu / Dian Ding / Lei Chen / |
PubMed 要旨 | ATP-sensitive potassium channels (K) are metabolic sensors that convert the intracellular ATP/ADP ratio to the excitability of cells. They are involved in many physiological processes and implicated ...ATP-sensitive potassium channels (K) are metabolic sensors that convert the intracellular ATP/ADP ratio to the excitability of cells. They are involved in many physiological processes and implicated in several human diseases. Here we present the cryo-EM structures of the pancreatic K channel in both the closed state and the pre-open state, resolved in the same sample. We observe the binding of nucleotides at the inhibitory sites of the Kir6.2 channel in the closed but not in the pre-open state. Structural comparisons reveal the mechanism for ATP inhibition and Mg-ADP activation, two fundamental properties of K channels. Moreover, the structures also uncover the activation mechanism of diazoxide-type K openers. |
リンク | Nat Commun / PubMed:35589716 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.96 - 3.19 Å |
構造データ | EMDB-32310, PDB-7w4o: EMDB-32311, PDB-7w4p: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-E2H: ChemComp-ATP: |
由来 |
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キーワード | TRANSPORT PROTEIN / KATP / Kir6.2 / SUR1 / NN414 / ADP / ATP |