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Interaction Between Human Angiogenin and the p53 TAD2 Domain and Its Implication for Inhibitor Discovery

Interaction Between Human Angiogenin and the p53 TAD2 Domain and Its Implication for Inhibitor Discovery

Kwon Joo Yeo, Jun-Goo Jee, Eunha Hwang, Eun-Hee Kim, Young Ho Jeon, Hae-Kap Cheong

FEBS Lett. 2017 Dec;591(23):3916-3925.

PMID: 29105754

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 31 RRR33 and 50 KRSIK54 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 31 RRR33 and 50 KRSIK54 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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR4248743	Angiogenin human			Price

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