C1抑制因子远端铰链区在C1s活性调节中的作用。
Role of the distal hinge region of C1-inhibitor in the regulation of C1s activity.
作者信息
He S, Yang J C, Tsang S, Sim R B, Whaley K
机构信息
Department of Microbiology and Immunology, Leicester University, UK.
出版信息
FEBS Lett. 1997 Aug 4;412(3):506-10. doi: 10.1016/s0014-5793(97)00803-x.
A synthetic peptide corresponding to residues 448-459 of C1-inhibitor (C1-inh) binds to C1s, is a non-competitive inhibitor of C1s activity and prevents formation of an SDS-stable C1s-C1-inh complex. Substitutions of residues Q452, Q453 or F455 in this peptide resulted in loss of C1s binding and inhibitory activity of the peptide. NMR analysis of the peptide showed an area of well-defined structure from E450 to F455. The side chains of Q452, Q453 and Q455 were exposed to the solvent and therefore available for C1s binding. The defined structure in the peptide is compatible with our computer model of the serpin domain of C1-inh.
一种与C1抑制因子（C1-inh）第448 - 459位残基对应的合成肽可与C1s结合，是C1s活性的非竞争性抑制剂，并可阻止SDS稳定的C1s - C1-inh复合物的形成。该肽中第452位谷氨酰胺（Q452）、第453位谷氨酰胺（Q453）或第455位苯丙氨酸（F455）残基的取代会导致该肽失去与C1s的结合能力及抑制活性。对该肽的核磁共振分析显示，从第450位谷氨酸（E450）到第455位苯丙氨酸（F455）存在结构明确的区域。Q452、Q453和Q455的侧链暴露于溶剂中，因此可用于与C1s结合。该肽中明确的结构与我们构建的C1-inh丝氨酸蛋白酶抑制剂结构域的计算机模型相符。
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