文献类型：期刊文献

英文题名：Structure-function analysis of human protein Ero1-Lα

作者：Chu, Yanyan[1];Yang, Charles[1,2];Chen, Xianjun[1,2];Zheng, Wenyun[1,2];Yang, Yi[1,2];Tang, Yun[1]

机构：[1]E China Univ Sci & Technol, Sch Pharm, Dept Pharmaceut Sci, Shanghai 200237, Peoples R China;[2]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2009

卷号：389

期号：4

起止页码：645

外文期刊名：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000271151100016)】；

基金：This work was supported by the Program for New Century Excellent Talents in University (Grant No. NCET-08-0774), the 863 High-Tech Project (Grant Nos. 2006AA020404 and 2006AA02Z160), the 111 Project (Grant No. B07023), Cultivation Fund of the Key Scientific and Technical Innovation Project Ministry of Education of China (Grant No. 706023), Shanghai Pujiang Program (Grant No. 07PJ14030), and NSFC (Grant Nos. 30500102 and 90713026).

语种：英文

外文关键词：Disulfide bond; Ero1-L alpha; Thioredoxin; Homology modeling; Structure-function analysis

摘要：Human Ero1-L alpha catalyzes the formation of disulfide bond and hence plays an essential role in protein folding. Understanding the mechanism of disulfide bond formation in mammals is important because of the involvement of protein inisfolding in conditions such as diabetes, arthritis, cancer, and aging. However, the crystal structure of the enzyme is not available yet, which seriously hinders the understanding of biological function of Ero1-L alpha. Based on the crystal structure of yeast Ero1p, a rational three-dimensional structural model of Ero1-L alpha was built and the characteristics of the enzyme were hence investigated. The characteristic similarities and differences between Ero1-L alpha and Ero1p were compared on the basis of computational and experimental results, providing the first insight into the structure-function relationships of the enzymes. Both calculation and experiment got the concordant conclusion that FAD binds more tightly with Ero1-L alpha than Ero1p. In addition, the probable electron transfer pathway was proposed on the basis of the structural models. (C) 2009 Elsevier Inc. All rights reserved.