Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, VIC 3800, Australia.
Curr Opin Struct Biol. 2012 Jun;22(3):342-9. doi: 10.1016/j.sbi.2012.04.008. Epub 2012 May 31.
The bacterial cholesterol dependent cytolysins (CDCs) and membrane attack complex/perforin-like proteins (MACPF) represent two major branches of a large, exceptionally diverged superfamily. Most characterized CDC/MACPF proteins form large pores that function in immunity, venoms, and pathogenesis. Extensive structural, biochemical and biophysical studies have started to address some of the questions surrounding how the soluble, monomeric form of these remarkable molecules recognize diverse targets and assemble into oligomeric membrane embedded pores. This review explores mechanistic similarities and differences in how CDCs and MACPF proteins form pores.
细菌胆固醇依赖性细胞溶素(CDCs)和膜攻击复合物/穿孔素样蛋白(MACPF)代表了一个非常多样化的超大家族的两个主要分支。大多数特征明确的 CDC/MACPF 蛋白形成大孔,在免疫、毒液和发病机制中发挥作用。广泛的结构、生化和生物物理研究已经开始解决一些围绕这些非凡分子的可溶性单体形式如何识别不同靶标并组装成镶嵌在膜中的寡聚体孔的问题。本综述探讨了 CDC 和 MACPF 蛋白形成孔的机制相似性和差异。