Prokaryotic and eukaryotic porins

被引:13
作者
Schirmer, Tilman [1 ]
Rosenbusch, Jurg P. [1 ]
机构
[1] Univ Basel, Bioctr, Klingelbergstr 70, CH-4056 Basel, Switzerland
基金
瑞士国家科学基金会;
关键词
D O I
10.1016/S0959-440X(05)80075-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Porins form water-filled, voltage-controlled channels across bacterial outer membranes. The trimeric protein resides within the hydrophobic membrane domain with unusual stability despite its hydrophilicity. Its channels are formed by beta-barrels (one per monomer) that consist of single antiparallel pleated sheets. This motif is found over a considerable evolutionary distance. The general significance of this folding pattern in membrane proteins can only be evaluated once more high-resolution structures have been determined.
引用
收藏
页码:539 / 545
页数:7
相关论文
共 66 条