Han Qing, Fu Yan, Zhou Hao, He Yingbo, Luo Yongzhang
Laboratory of Protein Chemistry, the Protein Science Laboratory of the Ministry of Education, Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing, PR China.
FEBS Lett. 2007 Jun 26;581(16):3027-32. doi: 10.1016/j.febslet.2007.05.058. Epub 2007 May 29.
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(II)-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(II)-binding peptide to the N-terminus of human endostatin makes this molecule more stable and cooperative in the presence of Zn(II).
内皮抑素具有紧密的结构，在N端有一个锌（II）结合位点（His1、His3、His11和Asp76）。在本研究中，研究了锌（II）结合对重组人内皮抑素折叠和稳定性的影响。结果表明，锌（II）结合在生理pH值下能很大程度地稳定内皮抑素的结构。在某些蛋白水解条件下，锌（II）结合也有助于维持内皮抑素N端的完整性，这对于内皮抑素保持稳定结构至关重要。此外，在人内皮抑素的N端设计一个额外的锌（II）结合肽，可使该分子在有锌（II）存在时更稳定且协同性更好。
