[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.