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Interaction between human angiogenin and the p53 TAD2 domain and its implication for inhibitor discovery

Authors
Yeo, Kwon JooJee, Jun-GooHwang, EunhaKim, Eun-HeeJeon, Young HoCheong, Hae-Kap
Issue Date
12월-2017
Publisher
WILEY
Keywords
angiogenesis; Angiogenin; p53
Citation
FEBS LETTERS, v.591, no.23, pp.3916 - 3925
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
591
Number
23
Start Page
3916
End Page
3925
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/81405
DOI
10.1002/1873-3468.12899
ISSN
0014-5793
Abstract
Interaction between angiogenin and the p53 TAD2 domain in cancer cells can inhibit the function of the p53 tumor suppressor and promote cell survival. Based on a model structure using NMR and mutational analysis, positively charged (RRR33)-R-31 and (KRSIK54)-K-50 motifs of human angiogenin were identified as p53-binding sites that could interact with negatively charged D48/E51 and E56 residues of the p53 TAD2 domain, respectively. These results suggest that (RRR33)-R-31 and (KRSIK54)-K-50 motifs of human angiogenin might play a critical role in the regulation of p53-mediated apoptosis and angiogenesis in cancer cells. This study identifies potential target sites for screening angiogenin-specific inhibitors that could not only inhibit p53 binding but could also simultaneously inhibit cell binding, internalization, DNA binding, and nuclear translocation of human angiogenin.
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