4UUJ

POTASSIUM CHANNEL KCSA-FAB WITH TETRAHEXYLAMMONIUM

4UUJ の概要

• エントリーDOI: 10.2210/pdb4uuj/pdb
• 分子名称: ANTIBODY FAB FRAGMENT LIGHT CHAIN, PHOSPHATE ION, ANTIBODY FAB FRAGMENT HEAVY CHAIN, ... (11 entities in total)
• 機能のキーワード: immune system-metal transport complex, quaternary ammonium, protein-antibody fab complex, ionic channel, ion transport, potassium channel, immune system/metal 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: 4UUJ
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60873.44

構造登録者

Lenaeus, M.J.,Burdette, D.,Wagner, T.,Focia, P.J.,Gross, A. (登録日: 2014-07-29, 公開日: 2014-08-27, 最終更新日: 2024-10-16)

主引用文献

Lenaeus, M.J.,Burdette, D.,Wagner, T.,Focia, P.J.,Gross, A.
Structures of Kcsa in Complex with Symmetrical Quaternary Ammonium Compounds Reveal a Hydrophobic Binding Site.
Biochemistry, 53:5365-, 2014

PubMed Abstract: Potassium channels allow for the passive movement of potassium ions across the cell membrane and are instrumental in controlling the membrane potential in all cell types. Quaternary ammonium (QA) compounds block potassium channels and have long been used to study the functional and structural properties of these channels. Here we describe the interaction between three symmetrical hydrophobic QAs and the prokaryotic potassium channel KcsA. The structures demonstrate the presence of a hydrophobic pocket between the inner helices of KcsA and provide insight into the binding site and blocking mechanism of hydrophobic QAs. The structures also reveal a structurally hidden pathway between the central cavity and the outside membrane environment reminiscent of the lateral fenestration observed in sodium channels that can be accessed through small conformational changes in the pore wall. We propose that the hydrophobic binding pocket stabilizes the alkyl chains of long-chain QA molecules and may play a key role in hydrophobic drug binding in general.

PubMed: 25093676
DOI: 10.1021/BI500525S

実験手法

X-RAY DIFFRACTION (2.4 Å)