7WIT
Structure of SUR1 in complex with mitiglinide
Summary for 7WIT
| Entry DOI | 10.2210/pdb7wit/pdb |
| EMDB information | 32535 |
| Descriptor | ATP-sensitive inward rectifier potassium channel 11,ATP-binding cassette sub-family C member 8 isoform X1, ADENOSINE-5'-TRIPHOSPHATE, (2S)-4-[(3aR,7aS)-1,3,3a,4,5,6,7,7a-octahydroisoindol-2-yl]-4-oxidanylidene-2-(phenylmethyl)butanoic acid (3 entities in total) |
| Functional Keywords | sur1, katp, channel, mitiglinide, membrane protein |
| Biological source | Bos taurus (cattle) More |
| Total number of polymer chains | 1 |
| Total formula weight | 160262.43 |
| Authors | Chen, L.,Wang, M.M. (deposition date: 2022-01-04, release date: 2022-11-16, Last modification date: 2024-06-26) |
| Primary citation | Wang, M.M.,Wu, J.X.,Chen, L. Structural Insights Into the High Selectivity of the Anti-Diabetic Drug Mitiglinide Front Pharmacol, 13:929684-929684, 2022 Cited by PubMed Abstract: 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. PubMed: 35847046DOI: 10.3389/fphar.2022.929684 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.21 Å) |
Structure validation
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