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


, : Contributions of Zn(II)-binding to the structural stability of endostatin. Febs Letters 581(16): 3027-3032

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).

US$19.90

PMID: 17544408

DOI: 10.1016/j.febslet.2007.05.058


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