Kemmink J, Darby N J, Dijkstra K, Nilges M, Creighton T E
European Molecular Biology Laboratory, Heidelberg, Germany.
Biochemistry. 1996 Jun 18;35(24):7684-91. doi: 10.1021/bi960335m.
As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
作为剖析人蛋白质二硫键异构酶（PDI）结构的第一步，已使用异核多维核磁共振技术确定了与其序列前120个残基相对应的片段的结构。从其一级结构同源性可以预期，该片段具有硫氧还蛋白折叠结构。它们结构上的异同有助于解释为什么硫氧还蛋白是还原剂，而PDI是蛋白质巯基的氧化剂。结果证实，PDI具有模块化的多结构域结构，这将有助于对其进行结构和功能表征。
