Prepore for a breakthrough

被引：25
作者：
Bayley, H [1 ]
Jayasinghe, L [1 ]
Wallace, M [1 ]
机构：
[1] Univ Oxford, Dept Chem, Chem Res Lab, Oxford OX1 3TA, England
来源：
NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2005年 / 12卷 / 05期
关键词：
D O I：
10.1038/nsmb0505-385
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：
A key to understanding bacterial pathogenicity is the mechanism by which water-soluble protein toxins assemble on cell membranes to form oligomeric bilayer-spanning pores. The recent reconstructions from cryo-electron micrographs of three-dimensional pore and prepore structures of the cholesterol-dependent toxin pneumolysin shed new light on the later steps of the assembly of large toxin pores.
引用
收藏
页码：385 / 386
页数：2
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