Doyle Declan A
Structural Genomics Consortium, University of Oxford, Botnar Research Centre, Oxford, OX3 7LD, UK.
Eur Biophys J. 2004 May;33(3):175-9. doi: 10.1007/s00249-003-0382-z. Epub 2004 Mar 16.
The recent crystal structure of the prokaryotic inwardly rectifying potassium channel, KirBac1.1, revealed for the first time the structure of a K+ channel in the closed state plus the location of the activation gate. Comparison of the KirBac1.1 structure with other known ion channels reveals a number of common structural features. These common characteristics include the formation of the ion conduction pathway at the interface between adjacent subunits, non-fixed charges forming part of the ion pathway, electrostatic sinks drawing ions into the channel, helix dipoles, and hydrophobic gates that ultimately prevent ion movement. This review describes in detail common structural themes present in ion channels.
原核内向整流钾通道KirBac1.1最近的晶体结构首次揭示了处于关闭状态的钾通道结构以及激活门的位置。将KirBac1.1的结构与其他已知离子通道进行比较，发现了许多共同的结构特征。这些共同特征包括在相邻亚基之间的界面处形成离子传导途径、构成离子通道一部分的非固定电荷、将离子吸入通道的静电阱、螺旋偶极子以及最终阻止离子移动的疏水门。本综述详细描述了离子通道中存在的常见结构主题。
