6MIE
Solution NMR structure of the KCNQ1 voltage-sensing domain
Summary for 6MIE
| Entry DOI | 10.2210/pdb6mie/pdb |
| NMR Information | BMRB: 30517 |
| Descriptor | Potassium voltage-gated channel subfamily KQT member 1 (1 entity in total) |
| Functional Keywords | ion channel, kcnq1, kv7.1, voltage sensor, potassium channel, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18184.63 |
| Authors | Taylor, K.C.,Kuenze, G.,Smith, J.A.,Meiler, J.,McFeeters, R.L.,Sanders, C.R. (deposition date: 2018-09-19, release date: 2020-03-04, Last modification date: 2024-05-01) |
| Primary citation | Taylor, K.C.,Kang, P.W.,Hou, P.,Yang, N.D.,Kuenze, G.,Smith, J.A.,Shi, J.,Huang, H.,White, K.M.,Peng, D.,George, A.L.,Meiler, J.,McFeeters, R.L.,Cui, J.,Sanders, C.R. Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state. Elife, 9:-, 2020 Cited by PubMed Abstract: Voltage-gated ion channels feature voltage sensor domains (VSDs) that exist in three distinct conformations during activation: resting, intermediate, and activated. Experimental determination of the structure of a potassium channel VSD in the intermediate state has previously proven elusive. Here, we report and validate the experimental three-dimensional structure of the human KCNQ1 voltage-gated potassium channel VSD in the intermediate state. We also used mutagenesis and electrophysiology in oocytes to functionally map the determinants of S4 helix motion during voltage-dependent transition from the intermediate to the activated state. Finally, the physiological relevance of the intermediate state KCNQ1 conductance is demonstrated using voltage-clamp fluorometry. This work illuminates the structure of the VSD intermediate state and demonstrates that intermediate state conductivity contributes to the unusual versatility of KCNQ1, which can function either as the slow delayed rectifier current (I) of the cardiac action potential or as a constitutively active epithelial leak current. PubMed: 32096762DOI: 10.7554/eLife.53901 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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