Kieffer B, Driscoll P C, Campbell I D, Willis A C, van der Merwe P A, Davis S J
Department of Biochemistry, University of Oxford, U.K.
Biochemistry. 1994 Apr 19;33(15):4471-82.
The cell surface antigen CD59 is an inhibitor of complement-mediated lysis and a member of the Ly6 superfamily (Ly6SF) of cysteine-rich cell-surface molecules whose sequences are related to those of snake venom neurotoxins. The three-dimensional solution structure of a recombinant form of the extracellular region of the molecule (residues 1-70 of the mature protein; sCD59) has been solved by 2D NMR methods. sCD59 is a relatively flat, disk-shaped molecule consisting of a two-standed beta-sheet finger loosely packed against a protein core formed by a three-stranded beta-sheet and a short helix. Structure calculations allowed an unambiguous assignment of the disulfide-bonded cysteine pairs as 3-26, 6-13, 19-39, 45-63, and 64-69. The topology of sCD59 is similar to that of the snake venom neurotoxins and consistent with an evolutionary relationship existing between the Ly6SF and the neurotoxins.
细胞表面抗原CD59是补体介导的细胞溶解的抑制剂，也是富含半胱氨酸的细胞表面分子Ly6超家族（Ly6SF）的成员，其序列与蛇毒神经毒素的序列相关。该分子细胞外区域的重组形式（成熟蛋白的1-70位残基；sCD59）的三维溶液结构已通过二维核磁共振方法解析。sCD59是一个相对扁平的盘状分子，由一个双股β-折叠指松散地堆积在由三股β-折叠和一个短螺旋形成的蛋白质核心上。结构计算明确确定了二硫键连接的半胱氨酸对为3-26、6-13、19-39、45-63和64-69。sCD59的拓扑结构与蛇毒神经毒素相似，并且与Ly6SF和神经毒素之间存在的进化关系一致。
