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TitleStructural Insights Into the High Selectivity of the Anti-Diabetic Drug Mitiglinide.
Journal, issue, pagesFront Pharmacol, Vol. 13, Page 929684, Year 2022
Publish dateJun 30, 2022
AuthorsMengmeng Wang / Jing-Xiang Wu / Lei Chen /
PubMed AbstractMitiglinide is a highly selective fast-acting anti-diabetic drug that induces insulin secretion by inhibiting pancreatic K channels. However, how mitiglinide binds K channels remains unknown. Here, ...Mitiglinide is a highly selective fast-acting anti-diabetic drug that induces insulin secretion by inhibiting pancreatic K channels. However, how mitiglinide binds K channels remains unknown. Here, we show the cryo-EM structure of the SUR1 subunit complexed with mitiglinide. The structure reveals that mitiglinide binds inside the common insulin secretagogue-binding site of SUR1, which is surrounded by TM7, TM8, TM16, and TM17. Mitiglinide locks SUR1 in the NBD-separated inward-facing conformation. The detailed structural analysis of the mitiglinide-binding site uncovers the molecular basis of its high selectivity.
External linksFront Pharmacol / PubMed:35847046 / PubMed Central
MethodsEM (single particle)
Resolution3.21 Å
Structure data

32535

7wit

EMDB-32535, PDB-7wit:
Structure of SUR1 in complex with mitiglinide
Method: EM (single particle) / Resolution: 3.21 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-9I0:
(2S)-4-[(3aR,7aS)-1,3,3a,4,5,6,7,7a-octahydroisoindol-2-yl]-4-oxidanylidene-2-(phenylmethyl)butanoic acid

Source
  • mesocricetus auratus (golden hamster)
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / SUR1 / KATP / channel / mitiglinide

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