3UKM
Crystal structure of the human two pore domain potassium ion channel K2P1 (TWIK-1)
Summary for 3UKM
| Entry DOI | 10.2210/pdb3ukm/pdb |
| Descriptor | Potassium channel subfamily K member 1, UNDECANE, POTASSIUM ION, ... (4 entities in total) |
| Functional Keywords | potassium channel, membrane protein, eukaryotic, two-pore domain potassium channel, k2p channel, membrane |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Multi-pass membrane protein (Potential): O00180 |
| Total number of polymer chains | 4 |
| Total formula weight | 128660.16 |
| Authors | Long, S.B.,Miller, A.N. (deposition date: 2011-11-09, release date: 2012-02-08, Last modification date: 2024-10-30) |
| Primary citation | Miller, A.N.,Long, S.B. Crystal structure of the human two-pore domain potassium channel K2P1. Science, 335:432-436, 2012 Cited by PubMed Abstract: Two-pore domain potassium (K(+)) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K(+) ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K(+) channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli. PubMed: 22282804DOI: 10.1126/science.1213274 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
Download full validation report
