Characterization of a mutant sulfonylurea receptor SUR2B with high affinity for sulfonylureas and openers: differences in the coupling to Kir6.x subtypes.

@article{Hambrock2001CharacterizationOA,
  title={Characterization of a mutant sulfonylurea receptor SUR2B with high affinity for sulfonylureas and openers: differences in the coupling to Kir6.x subtypes.},
  author={Annette Hambrock and Cornelia L{\"o}ffler-Walz and Ulrich Russ and Ulf Lange and Ulrich Quast},
  journal={Molecular pharmacology},
  year={2001},
  volume={60 1},
  pages={
          190-9
        }
}
ATP-dependent K(+) channels are composed of pore-forming subunits of the Kir6.x family and of sulfonylurea receptors (SURs). SUR1, expressed in pancreatic beta-cells, has a higher affinity for sulfonylureas, such as glibenclamide, than SUR2B, expressed in smooth muscle. This difference is mainly caused by serine 1237 in SUR1 corresponding to tyrosine 1206 in SUR2B. To increase the affinity of SUR2B for glibenclamide, the mutant SUR2B(Y1206S) was constructed. In whole-cell patch-clamp… CONTINUE READING

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A single residue in SURs is essential for sulphonylurea binding

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Highly Influential
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