Anderluh Gregor, Lakey Jeremy H
Department of Biology, Biotechnical Faculty, University of Ljubljana, Vecna pot 111, 1000, Ljubljana, Slovenia.
Trends Biochem Sci. 2008 Oct;33(10):482-90. doi: 10.1016/j.tibs.2008.07.004. Epub 2008 Sep 6.
Membrane disruption can efficiently alter cellular function; indeed, pore-forming toxins (PFTs) are well known as important bacterial virulence factors. However, recent data have revealed that structures similar to those found in PFTs are found in membrane active proteins across disparate phyla. Many similarities can be identified only at the 3D-structural level. Of note, domains found in membrane-attack complex proteins of complement and perforin (MACPF) resemble cholesterol-dependent cytolysins from Gram-positive bacteria, and the Bcl family of apoptosis regulators share similar architectures with Escherichia coli pore-forming colicins. These and other correlations provide considerable help in understanding the structural requirements for membrane binding and pore formation.
膜破坏可有效改变细胞功能；实际上，成孔毒素（PFTs）作为重要的细菌毒力因子广为人知。然而，最近的数据显示，在不同门类的膜活性蛋白中发现了与PFTs中发现的结构相似的结构。许多相似之处只能在三维结构水平上识别。值得注意的是，补体和穿孔素的膜攻击复合物蛋白（MACPF）中发现的结构域类似于革兰氏阳性菌的胆固醇依赖性细胞溶素，凋亡调节因子的Bcl家族与大肠杆菌成孔大肠杆菌素具有相似的结构。这些以及其他相关性为理解膜结合和孔形成的结构要求提供了相当大的帮助。
