What is it about?
The role of the aminopeptidase N dynamics in its function as coronavirus receptor, proving how to inhibit coronavirus infections with drugs that target their entry receptor molecules.
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Why is it important?
We describe how APN moves and functions, as well as a new ways to inhibit this moonlighting enzyme. In addition, we demostrate that coronavirus receptor active sites-binding drugs can be used to prevent virus cell entry. This is the first report showing that coronavirus cell infection can be inhibited by drugs toward thelr entry receptor, which can guide the design of ACE2-binding drugs that prevent the COVID-19 disease.
Perspectives
APN is an important target for cancer chemotherapy. We report several crystal structures of the mammalian aminopeptidase N (APN) that define the dynamic conformation of this ectoenzyme. APN is a moonlighting protein involved in multiple biological processes, cancer and coronavirus infections. Our results couple APN functions with distinct conformations of its ectodomain, demonstrating allosteric inhibition of APN catalysis and virus infection through the suppression of protein motions. We demostrate that drugs that bind with high affinity to the active site of coronavirus receptors can be use to inhibit coronavirus cell entry and infections.
Professor Jose M Casasnovas
CNB-CSIC
Read the Original
This page is a summary of: Allosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection, Scientific Reports, April 2017, Springer Science + Business Media,
DOI: 10.1038/srep46045.
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