3TCU

Crystal Structure of NaK2K Channel D68E Mutant

3TCU の概要

• エントリーDOI: 10.2210/pdb3tcu/pdb
• 関連するPDBエントリー: 3OUF 3T4D 3T4Z
• 分子名称: Potassium channel protein, POTASSIUM ION (3 entities in total)
• 機能のキーワード: membrane protein, ion channel
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21884.18

構造登録者

Sauer, D.B.,Zeng, W.,Raghunathan, S.,Jiang, Y. (登録日: 2011-08-09, 公開日: 2011-10-05, 最終更新日: 2024-02-28)

主引用文献

Sauer, D.B.,Zeng, W.,Raghunathan, S.,Jiang, Y.
Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation.
Proc.Natl.Acad.Sci.USA, 108:16634-16639, 2011

PubMed Abstract: The structural and functional conversion of the nonselective NaK channel to a K(+) selective channel (NaK2K) allows us to identify two key residues, Tyr and Asp in the filter sequence of TVGYGD, that participate in interactions central to stabilizing the K(+) channel selectivity filter. By using protein crystallography and channel electrophysiology, we demonstrate that the K(+) channel filter exists as an energetically strained structure and requires these key protein interactions working in concert to hold the filter in the precisely defined four-sited configuration that is essential for selective K(+) permeation. Disruption of either interaction, as tested on both the NaK2K and eukaryotic K(v)1.6 channels, can reduce or completely abolish K(+) selectivity and in some cases may also lead to channel inactivation due to conformational changes at the filter. Additionally, on the scaffold of NaK we recapitulate the protein interactions found in the filter of the Kir channel family, which uses a distinct interaction network to achieve similar stabilization of the filter.

PubMed: 21933962
DOI: 10.1073/pnas.1111688108

実験手法

X-RAY DIFFRACTION (1.75 Å)