9TFV
Cryo-EM structure of the inward rectifying potassium channel 7.1 (Kir7.1)
Summary for 9TFV
| Entry DOI | 10.2210/pdb9tfv/pdb |
| EMDB information | 55878 |
| Descriptor | Inward rectifier potassium channel 13, POTASSIUM ION (2 entities in total) |
| Functional Keywords | potassium ion channel, active conformation, human membrane protein, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 166920.37 |
| Authors | O'Malley, N.,Faust, B.,Nasrallah, C.,Wallace, B.A. (deposition date: 2025-11-27, release date: 2026-07-01, Last modification date: 2026-07-08) |
| Primary citation | O'Malley, N.,Nasrallah, C.,Churchill, A.,Bertrand, J.,Faust, B.R.,Wallace, B.A. Cryo-EM structure of the human Kir7.1 channel reveals the molecular basis of snowflake vitreoretinal degeneration disease. Commun Biol, 2026 Cited by PubMed Abstract: The inward rectifying human potassium channel 7.1 (Kir7.1) is a vital ion channel involved in maintaining cellular homoeostasis and electrical signalling across various tissues and organs, activated by phosphatidylinositol 4,5-bisphosphate (PIP). A genetically inherited loss-of-function mutation in Kir7.1 (R162W) has been linked to the rare retinal disease Snowflake Vitreoretinal Degeneration (SVD), for which there are currently no curative treatment options. Here, the cryo-EM structures of wild type Kir7.1 and the R162W disease-related variant are presented, which unveil the molecular basis of SVD: the reorientation of the mutant tryptophan side chains into the pore impedes the flow of potassium ions, which would result in the loss of Kir7.1 transport function. Furthermore, this investigation shows that PIP binding widens the helix bundle crossing gate diameter, even in the absence of a docked cytoplasmic domain. This observation contrasts with other Kir-PIP₂ complexes and suggests that Kir7.1 may adopt an intermediate conformation during channel activation. These findings provide a structural basis for Kir7.1 loss of function in SVD and provide a framework for future therapeutic development. PubMed: 42324408DOI: 10.1038/s42003-026-10436-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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