ATP-sensitive potassium channels (KATP) play crucial roles in many essential physiological processes and have been implicated extensively in a spectrum of metabolic diseases and disorders. This article describes the structure of a hetero-octameric pancreatic KATP channel in complex with a non-competitive inhibitor glibenclamide by single-particle cryoelectron microscopy to 5.6-Å resolution. Glibenclamide-bound SUR1 uses TMD0-L0 fragment to stabilize Kir6.2 channel in a closed conformation. In another structural population, a putative co-purified phosphatidylinositol 4,5-bisphosphate (PIP2) molecule uncouples Kir6.2 from glibenclamide-bound SUR1. These structural observations suggest a molecular mechanism for KATP regulation by anti-diabetic sulfonylurea drugs, intracellular adenosine nucleotide concentrations, and PIP2 lipid.
 Li et al. (2017). Cell 168(1-2):101-110. Structure of a Pancreatic ATP-Sensitive Potassium Channel. [PMID: 28086082]
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