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Title | Structural insights into the mechanism of pancreatic K channel regulation by nucleotides. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 2770, Year 2022 |
Publish date | May 19, 2022 |
Authors | Mengmeng Wang / Jing-Xiang Wu / Dian Ding / Lei Chen / |
PubMed Abstract | 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. |
External links | Nat Commun / PubMed:35589716 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.96 - 3.19 Å |
Structure data | EMDB-32310, PDB-7w4o: EMDB-32311, PDB-7w4p: |
Chemicals | ChemComp-ADP: ChemComp-MG: ChemComp-E2H: ChemComp-ATP: |
Source |
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Keywords | TRANSPORT PROTEIN / KATP / Kir6.2 / SUR1 / NN414 / ADP / ATP |