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本文引用的文献

1
Improved high-level expression system for eukaryotic genes in Escherichia coli using T7 RNA polymerase and rare ArgtRNAs.利用T7 RNA聚合酶和稀有精氨酸tRNA改进大肠杆菌中真核基因的高效表达系统。
Biotechniques. 1995 Aug;19(2):196-8, 200.
2
Redox properties of protein disulfide isomerase (DsbA) from Escherichia coli.大肠杆菌蛋白质二硫键异构酶（DsbA）的氧化还原特性
Protein Sci. 1993 May;2(5):717-26. doi: 10.1002/pro.5560020503.
3
The reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.DsbA的反应性和不稳定二硫键，DsbA是一种在体内蛋白质二硫键形成所需的蛋白质。
Biochemistry. 1993 May 18;32(19):5083-92. doi: 10.1021/bi00070a016.
4
Crystal structure of the DsbA protein required for disulphide bond formation in vivo.体内二硫键形成所需的DsbA蛋白的晶体结构。
Nature. 1993 Sep 30;365(6445):464-8. doi: 10.1038/365464a0.
5
Reactivity and ionization of the active site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.DsbA（一种在体内形成二硫键所需的蛋白质）活性位点半胱氨酸残基的反应性和离子化作用。
Biochemistry. 1994 May 17;33(19):5974-83. doi: 10.1021/bi00185a039.
6
Mutations in the thioredoxin sites of protein disulfide isomerase reveal functional nonequivalence of the N- and C-terminal domains.蛋白质二硫键异构酶硫氧还蛋白位点的突变揭示了N端和C端结构域的功能不等效性。
J Biol Chem. 1994 Dec 9;269(49):30946-52.
7
Protein disulphide isomerase: building bridges in protein folding.蛋白质二硫键异构酶：在蛋白质折叠中搭建桥梁
Trends Biochem Sci. 1994 Aug;19(8):331-6. doi: 10.1016/0968-0004(94)90072-8.
8
The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins.人类雌激素受体与DNA的相互作用受受体相关蛋白的调节。
Mol Endocrinol. 1994 Oct;8(10):1407-19. doi: 10.1210/mend.8.10.7854357.
9
Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.蛋白质二硫键异构酶各个硫氧还蛋白样结构域的功能特性。
Biochemistry. 1995 Sep 19;34(37):11725-35. doi: 10.1021/bi00037a009.
10
Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins.相敏二维相关光谱法（COSY）在蛋白质中¹H-¹H自旋-自旋耦合常数测量中的应用。
Biochem Biophys Res Commun. 1983 Jun 29;113(3):967-74. doi: 10.1016/0006-291x(83)91093-8.

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.

DOI:10.1002/pro.5560041216
PMID:8580850
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2143042/
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。