7LJB
Human TRAAK K+ channel mutant G158D in a K+ bound conductive conformation
Summary for 7LJB
| Entry DOI | 10.2210/pdb7ljb/pdb |
| Descriptor | Isoform 2 of Potassium channel subfamily K member 4, ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT LIGHT CHAIN, ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT HEAVY CHAIN, ... (6 entities in total) |
| Functional Keywords | potassium ion channel, metal transport, metal transport-immune system complex, metal transport/immune system |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 158635.76 |
| Authors | Rietmeijer, R.A.,Brohawn, S.G. (deposition date: 2021-01-28, release date: 2021-06-30, Last modification date: 2024-11-06) |
| Primary citation | Rietmeijer, R.A.,Sorum, B.,Li, B.,Brohawn, S.G. Physical basis for distinct basal and mechanically gated activity of the human K + channel TRAAK. Neuron, 109:2902-2913.e4, 2021 Cited by PubMed Abstract: TRAAK is a mechanosensitive two-pore domain K (K2P) channel localized to nodes of Ranvier in myelinated neurons. TRAAK deletion in mice results in mechanical and thermal allodynia, and gain-of-function mutations cause the human neurodevelopmental disorder FHEIG. TRAAK displays basal and stimulus-gated activities typical of K2Ps, but the mechanistic and structural differences between these modes are unknown. Here, we demonstrate that basal and mechanically gated openings are distinguished by their conductance, kinetics, and structure. Basal openings are low conductance, short duration, and due to a conductive channel conformation with the interior cavity exposed to the surrounding membrane. Mechanically gated openings are high conductance, long duration, and due to a channel conformation in which the interior cavity is sealed to the surrounding membrane. Our results explain how dual modes of activity are produced by a single ion channel and provide a basis for the development of state-selective pharmacology with the potential to treat disease. PubMed: 34390650DOI: 10.1016/j.neuron.2021.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.97 Å) |
Structure validation
Download full validation report
