蛋白质二硫键异构酶N端硫氧还蛋白样结构域的核磁共振表征
Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase.
作者信息
Kemmink J, Darby N J, Dijkstra K, Scheek R M, Creighton T E
机构信息
European Molecular Biology Laboratory, Heidelberg, Germany.
出版信息
Protein Sci. 1995 Dec;4(12):2587-93. doi: 10.1002/pro.5560041216.
Abstract
A genetically engineered protein consisting of the 120 residues at the N-terminus of human protein disulfide isomerase (PDI) has been characterized by 1H, 13C, and 15N NMR methods. The sequence of this protein is 35% identical to Escherichia coli thioredoxin, and it has been found also to have similar patterns of secondary structure and beta-sheet topology. The results confirm that PDI is a modular, multidomain protein. The last 20 residues of the N-terminal domain of PDI are some of those that are similar to part of the estrogen receptor, yet they appear to be an intrinsic part of the thioredoxin fold. This observation makes it unlikely that any of the segments of PDI with similarities to the estrogen receptor comprise individual domains.
摘要
一种由人蛋白质二硫键异构酶（PDI）N端120个残基组成的基因工程蛋白已通过1H、13C和15N核磁共振方法进行了表征。该蛋白的序列与大肠杆菌硫氧还蛋白有35%的同一性，并且还发现其具有相似的二级结构模式和β-折叠拓扑结构。结果证实PDI是一种模块化的多结构域蛋白。PDI N端结构域的最后20个残基是与雌激素受体部分相似的一些残基，但它们似乎是硫氧还蛋白折叠的固有部分。这一观察结果使得PDI中与雌激素受体相似的任何片段都不太可能构成独立的结构域。
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