2ATK

Structure of a mutant KcsA K+ channel

2ATK の概要

• エントリーDOI: 10.2210/pdb2atk/pdb
• 関連するPDBエントリー: 1ZWI
• 分子名称: ANTIBODY FAB FRAGMENT HEAVY CHAIN, ANTIBODY FAB FRAGMENT LIGHT CHAIN, Voltage-gated potassium channel, ... (6 entities in total)
• 機能のキーワード: k+ channel, mutant kcsa, protein-antibody fab complex, immune system-ion transport complex, immune system/ion transport
• 由来する生物種: Mus musculus (house 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: 60418.47

構造登録者

Cordero-Morales, J.F.,Cuello, L.G.,Zhao, Y.,Jogini, V.,Chakrapani, S.,Roux, B.,Perozo, E. (登録日: 2005-08-25, 公開日: 2006-03-07, 最終更新日: 2024-10-23)

主引用文献

Cordero-Morales, J.F.,Cuello, L.G.,Zhao, Y.,Jogini, V.,Cortes, D.M.,Roux, B.,Perozo, E.
Molecular determinants of gating at the potassium-channel selectivity filter.
Nat.Struct.Mol.Biol., 13:311-318, 2006

PubMed Abstract: We show that in the potassium channel KcsA, proton-dependent activation is followed by an inactivation process similar to C-type inactivation, and this process is suppressed by an E71A mutation in the pore helix. EPR spectroscopy demonstrates that the inner gate opens maximally at low pH regardless of the magnitude of the single-channel-open probability, implying that stationary gating originates mostly from rearrangements at the selectivity filter. Two E71A crystal structures obtained at 2.5 A reveal large structural excursions of the selectivity filter during ion conduction and provide a glimpse of the range of conformations available to this region of the channel during gating. These data establish a mechanistic basis for the role of the selectivity filter during channel activation and inactivation.

PubMed: 16532009
DOI: 10.1038/nsmb1069

実験手法

X-RAY DIFFRACTION (2.5 Å)