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


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). Study holds ProTherm entries: 22884, 22885, 22886, 22887, 22888, 22889, 22890, 22891, 22892, 22893, 22894 Extra Details: apo form; The heating rate is 0.5 degreesC/min Endostatin; Zn(II)-binding; Stability; Protein folding; Zn(II)-binding peptide

Submission Details

ID: jHjQPbJc3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:53 p.m.

Version: 1

Publication Details
Han Q;Fu Y;Zhou H;He Y;Luo Y,FEBS Lett. (2007) Contributions of Zn(II)-binding to the structural stability of endostatin. PMID:17544408
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Collagen alpha-1(XVIII) chain P39060 COIA1_HUMAN