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3OGC

KcsA E71A variant in presence of Na+

3OGC の概要
エントリーDOI10.2210/pdb3ogc/pdb
分子名称antibody Fab fragment heavy chain, antibody Fab fragment light chain, Voltage-gated potassium channel, ... (4 entities in total)
機能のキーワードvoltage-gated channel, antibody fab complex, membrane protein
由来する生物種Mus musculus (mouse)
詳細
細胞内の位置Cell membrane; Multi-pass membrane protein: P0A334
タンパク質・核酸の鎖数3
化学式量合計60998.52
構造登録者
McCoy, J.G.,Nimigean, C.M. (登録日: 2010-08-16, 公開日: 2011-03-16, 最終更新日: 2024-11-27)
主引用文献Cheng, W.W.,McCoy, J.G.,Thompson, A.N.,Nichols, C.G.,Nimigean, C.M.
Mechanism for selectivity-inactivation coupling in KcsA potassium channels.
Proc.Natl.Acad.Sci.USA, 108:5272-5277, 2011
Cited by
PubMed Abstract: Structures of the prokaryotic K(+) channel, KcsA, highlight the role of the selectivity filter carbonyls from the GYG signature sequence in determining a highly selective pore, but channels displaying this sequence vary widely in their cation selectivity. Furthermore, variable selectivity can be found within the same channel during a process called C-type inactivation. We investigated the mechanism for changes in selectivity associated with inactivation in a model K(+) channel, KcsA. We found that E71A, a noninactivating KcsA mutant in which a hydrogen-bond behind the selectivity filter is disrupted, also displays decreased K(+) selectivity. In E71A channels, Na(+) permeates at higher rates as seen with and flux measurements and analysis of intracellular Na(+) block. Crystal structures of E71A reveal that the selectivity filter no longer assumes the "collapsed," presumed inactivated, conformation in low K(+), but a "flipped" conformation, that is also observed in high K(+), high Na(+), and even Na(+) only conditions. The data reveal the importance of the E71-D80 interaction in both favoring inactivation and maintaining high K(+) selectivity. We propose a molecular mechanism by which inactivation and K(+) selectivity are linked, a mechanism that may also be at work in other channels containing the canonical GYG signature sequence.
PubMed: 21402935
DOI: 10.1073/pnas.1014186108
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.8 Å)
構造検証レポート
Validation report summary of 3ogc
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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