Williams Marni, Baxter Richard
Department. of Chemistry, Yale University, New Haven, CT, USA.
Biophys Rev. 2014 Dec;6(3-4):261-272. doi: 10.1007/s12551-014-0142-6. Epub 2014 Jul 19.
Thioester-containing proteins (TEPs) form an ancient and diverse family of secreted proteins that play central roles in the innate immune response. Two families of TEPs, complement factors and α-macroglobulins, have been known and studied in vertebrates for many years, but only in the last decade have crystal structures become available. In the same period, the presence of two additional classes of TEPs has been revealed in arthropods. In this review, we discuss the common structural features TEPs and how this knowledge can be applied to the many arthropod TEPs of unknown function. TEPs perform a wide variety of functions that are driven by different quaternary structures and protein-protein interactions between a common set of folded domains. A common theme is regulated conformational change triggered by proteolysis. Structure-function analysis of the diverse arthropod TEPs may identify not just new mechanisms in innate immunity but also interfaces between immunity, development and cell death.
含硫酯蛋白（TEPs）构成了一个古老且多样的分泌蛋白家族，在先天免疫反应中发挥核心作用。在脊椎动物中，两类含硫酯蛋白，即补体因子和α-巨球蛋白，多年来已为人所知并得到研究，但直到最近十年才有了晶体结构。同一时期，在节肢动物中发现了另外两类含硫酯蛋白。在这篇综述中，我们讨论了含硫酯蛋白的共同结构特征，以及如何将这些知识应用于许多功能未知的节肢动物含硫酯蛋白。含硫酯蛋白执行多种功能，这些功能由不同的四级结构以及一组常见折叠结构域之间的蛋白质-蛋白质相互作用驱动。一个共同的主题是由蛋白水解引发的构象变化调控。对多种节肢动物含硫酯蛋白的结构-功能分析不仅可能揭示先天免疫中的新机制，还可能揭示免疫、发育和细胞死亡之间的联系。
