Apr 5, 2020

Topological Analysis of SARS CoV-2 Main Protease

BioRxiv : the Preprint Server for Biology
Ernesto Estrada

Abstract

There is an urgent necessity of effective medication against SARS CoV-2, which is producing the COVID-19 pandemic across the world. Its main protease (Mpro) represents an attractive pharmacological target due to its involvement in essential viral functions. The crystal structure of free Mpro shows a large structural resemblance with the main protease of CoV-1. Here we report that CoV-2 Mpro is however 300% more sensitive than CoV-1 Mpro in transmitting tiny structural changes across the whole protein through long-range interactions. The largest sensitivity of Mpro to structural perturbations is located exactly around the catalytic site Cyst-145, and coincides with the binding site of several of its inhibitors. These findings, based on a simplified representation of the protein as a residue network, may help in designing potent inhibitors of CoV-2 Mpro.

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Mentioned in this Paper

Transposase
Replicative Transposition, DNA-mediated
Genome
Genes
Enzymes, antithrombotic
Terminal Repeat Sequences
PGBD5 gene
Excision
Site
Genomics

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