Contributions of Zn(II)-binding to the structural stability of endostatin

被引:78
作者
Han, Qing
Fu, Yan
Zhou, Hao
He, Yingbo
Luo, Yongzhang [1 ]
机构
[1] Tsing Hua Univ, Dept Biol Sci & Biotechnol, Prot Sci Lab Minist Educ, Prot Chem Lab, Beijing 100084, Peoples R China
[2] Washington Univ, Sch Med, Dept Cell Biol & Physiol, St Louis, MO 63110 USA
来源
FEBS LETTERS | 2007年 / 581卷 / 16期
基金
中国国家自然科学基金;
关键词
endostatin; Zn(II)-binding; stability; protein folding; Zn(II)-binding peptide;
D O I
10.1016/j.febslet.2007.05.058
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Endostatin has a compact structure with a Zn(II)-binding site (His1, His3, His11, and Asp76) at the N-terminus. In this study, the effects of Zn(II)-binding on the folding and stability of recombinant human endostatin were studied. The results show that Zn(Il)-binding largely stabilizes the structure of endostatin at physiological pH. Under some proteolytic conditions, Zn(II)-binding also contributes to the integrity of the N-terminus of endostatin, which is critical for endostatin to maintain a stable structure. Moreover, engineering an extra Zn(Il)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II). (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:3027 / 3032
页数:6
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