6MIE

Solution NMR structure of the KCNQ1 voltage-sensing domain

6MIE の概要

• エントリーDOI: 10.2210/pdb6mie/pdb
• NMR情報: BMRB: 30517
• 分子名称: Potassium voltage-gated channel subfamily KQT member 1 (1 entity in total)
• 機能のキーワード: ion channel, kcnq1, kv7.1, voltage sensor, potassium channel, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18184.63

構造登録者

Taylor, K.C.,Kuenze, G.,Smith, J.A.,Meiler, J.,McFeeters, R.L.,Sanders, C.R. (登録日: 2018-09-19, 公開日: 2020-03-04, 最終更新日: 2024-05-01)

主引用文献

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

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: 32096762
DOI: 10.7554/eLife.53901

実験手法

SOLUTION NMR