Lukoyanova Natalya, Saibil Helen R
Department of Crystallography and Institute of Structural Molecular Biology, Birkbeck College, London, UK.
Trends Immunol. 2008 Feb;29(2):51-3. doi: 10.1016/j.it.2007.11.003. Epub 2008 Jan 8.
Two recent crystal structures of membrane attack complex/perforin (MACPF) domains found in the complement and perforin families unexpectedly reveal that some proteins of the immune system share a common core fold with their bacterial targets. Although a relationship between MACPF proteins and the previously characterized bacterial cholesterol-dependent cytolysins (CDCs) is not detectable by sequence analysis, the MACPF structures show that eukaryotic defense and bacterial CDC attack share a common mechanism of membrane insertion and pore formation.
最近在补体和穿孔素家族中发现的膜攻击复合物/穿孔素(MACPF)结构域的两个晶体结构意外地揭示,免疫系统的一些蛋白质与其细菌靶点具有共同的核心折叠。尽管通过序列分析无法检测到MACPF蛋白与先前已鉴定的细菌胆固醇依赖性细胞溶素(CDC)之间的关系,但MACPF结构表明,真核防御和细菌CDC攻击共享膜插入和孔形成的共同机制。