6XIT
Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in complex with PIP2
Summary for 6XIT
| Entry DOI | 10.2210/pdb6xit/pdb |
| Related | 6XIS |
| EMDB information | 22199 22200 |
| Descriptor | G protein-activated inward rectifier potassium channel 2, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, POTASSIUM ION (3 entities in total) |
| Functional Keywords | g protein-coupled inwardly rectifying potassium channels, pip2, membrane protein |
| Biological source | Mus musculus (Mouse) |
| Total number of polymer chains | 4 |
| Total formula weight | 159351.39 |
| Authors | Niu, Y.,Tao, X.,MacKinnon, R. (deposition date: 2020-06-21, release date: 2020-10-07, Last modification date: 2024-10-23) |
| Primary citation | Niu, Y.,Tao, X.,Touhara, K.K.,MacKinnon, R. Cryo-EM analysis of PIP 2 regulation in mammalian GIRK channels. Elife, 9:-, 2020 Cited by PubMed Abstract: G-protein-gated inward rectifier potassium (GIRK) channels are regulated by G proteins and PIP. Here, using cryo-EM single particle analysis we describe the equilibrium ensemble of structures of neuronal GIRK2 as a function of the C8-PIP concentration. We find that PIP shifts the equilibrium between two distinguishable structures of neuronal GIRK (GIRK2), extended and docked, towards the docked form. In the docked form the cytoplasmic domain, to which G binds, becomes accessible to the cytoplasmic membrane surface where G resides. Furthermore, PIP binding reshapes the G binding surface on the cytoplasmic domain, preparing it to receive G. We find that cardiac GIRK (GIRK1/4) can also exist in both extended and docked conformations. These findings lead us to conclude that PIP influences GIRK channels in a structurally similar manner to Kir2.2 channels. In Kir2.2 channels, the PIP-induced conformational changes open the pore. In GIRK channels, they prepare the channel for activation by G. PubMed: 32844743DOI: 10.7554/eLife.60552 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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