Crowther D C, Evans D L, Carrell R W
Haematology Department, University of Cambridge, UK.
Curr Opin Biotechnol. 1992 Aug;3(4):399-407. doi: 10.1016/0958-1669(92)90169-j.
The serpins are unique among the families of serine proteinase inhibitors in having a reactive centre that is situated on a mobile loop. The structures of three alternative conformations are now known, and it can be deduced that the active form involves the partial insertion of the loop into the A sheet of the molecule. The ability of the loop to move in and out of this sheet has been adapted by evolution to allow the modulation of inhibitory activity. Manipulation of the structure of the loop and of other functional domains in the serpin superfamily enables the production of serpins with tailor-made activities. The ability of the loop to lock in latent conformations or to take part in intermolecular polymerization has implications for the production and stabilization of recombinant serpins. This review has been adapted from Current Opinion in Structural Biology 1992, 2:438-446.
丝氨酸蛋白酶抑制剂家族中，丝氨酸蛋白酶抑制剂（serpins）独具特色，其反应中心位于一个可移动的环上。目前已知三种不同构象的结构，由此可以推断，活性形式涉及该环部分插入分子的A片层。环进出该片层的移动能力在进化过程中得以适应，从而实现抑制活性的调节。对丝氨酸蛋白酶抑制剂超家族中环结构和其他功能域的操控，能够生产出具有定制活性的丝氨酸蛋白酶抑制剂。环锁定潜在构象或参与分子间聚合的能力，对重组丝氨酸蛋白酶抑制剂的生产和稳定具有重要意义。本综述改编自《结构生物学当前观点》1992年第2卷，第438 - 446页。
