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The primary function of the sulfonylurea receptor is to sense intracellular levels of the nucleotides ATP and ADP and in response facilitate the open or closing its associated Kir6.
SUR1 is an ATP-binding cassette (ABC) transporter with a novel function. In contrast to other ABC proteins, it serves as the regulatory subunit of an ion channel. The ATP-sensitive (KATP) channel is an octameric complex of four pore-forming Kir6.
Sulfonylureas are widely used to treat non- dependent diabetes mellitus. These drugs exert their hypoglycaemic effects by stimulating secretion from the pancreatic beta-cell.
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SUR1 contains two nucleotide-binding folds plus high affinity binding sites for therapeutic sulfonylurea drugs and related compounds. Drugs such as glibenclamide () and repaglinide bind with subnanomolar or nanomolar affinity and are potent inhibitors of SUR1-regulated channel activity (Table 1).

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