Hudson Andrew M, Cooley Lynn
Department of Genetics, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
Subcell Biochem. 2008;48:6-19. doi: 10.1007/978-0-387-09595-0_2.
The beta-propeller domain is a widespread protein organizational motif. Typically, beta-propeller proteins are encoded by repeated sequences where each repeat unit corresponds to a twisted beta-sheet structural motif; these beta-sheets are arranged in a circle around a central axis to generate the beta-propeller structure. Two superfamilies of beta-propeller proteins, the WD-repeat and Kelch-repeat families, exhibit similarities not only in structure, but, remarkably, also in the types of molecular functions they perform. While it is unlikely that WD and Kelch repeats evolved from a common ancestor, their evolution into diverse families of similar function may reflect the evolutionary advantages of the stable core beta-propeller fold. In this chapter, we examine the relationships between these two widespread protein families, emphasizing recently published work relating to the structure and function of both Kelch and WD-repeat proteins.
β-螺旋桨结构域是一种广泛存在的蛋白质组织基序。通常，β-螺旋桨蛋白由重复序列编码，其中每个重复单元对应一个扭曲的β-折叠结构基序；这些β-折叠围绕中心轴呈环状排列，形成β-螺旋桨结构。β-螺旋桨蛋白的两个超家族，即WD重复和kelch重复家族，不仅在结构上相似，而且在它们执行的分子功能类型上也显著相似。虽然WD和kelch重复不太可能从共同祖先进化而来，但它们进化成功能相似的不同家族可能反映了稳定的核心β-螺旋桨折叠的进化优势。在本章中，我们研究这两个广泛存在的蛋白质家族之间的关系，重点关注最近发表的与kelch和WD重复蛋白的结构和功能相关的研究。
