Structural highlights
Function
A0A1U8CME7_MESAU A2VDS4_BOVIN
Publication Abstract from PubMed
Mitiglinide is a highly selective fast-acting anti-diabetic drug that induces insulin secretion by inhibiting pancreatic KATP channels. However, how mitiglinide binds KATP 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.
Structural Insights Into the High Selectivity of the Anti-Diabetic Drug Mitiglinide.,Wang M, Wu JX, Chen L Front Pharmacol. 2022 Jun 30;13:929684. doi: 10.3389/fphar.2022.929684., eCollection 2022. PMID:35847046[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wang M, Wu JX, Chen L. Structural Insights Into the High Selectivity of the Anti-Diabetic Drug Mitiglinide. Front Pharmacol. 2022 Jun 30;13:929684. doi: 10.3389/fphar.2022.929684., eCollection 2022. PMID:35847046 doi:http://dx.doi.org/10.3389/fphar.2022.929684
