What is it about?
The SARS-CoV-2 main protease (Mpro) is a key enzyme in coronavirus replication, making it an important target for COVID-19 antiviral drug design. In this publication we show the atomic structure of Mpro at temperatures ranging from cryogenic to physiological, exploring how correlated structural movements may inform function.
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Why is it important?
Our data reveal a network of subtle but provocative temperature-dependent conformational diversity spanning several functionally relevant sites throughout Mpro. These findings are significant as they may motivate the design of antiviral drugs that target Mpro in regions other than the active site, which importantly could aid in preparation for future coronavirus pandemics.
Perspectives
All aspects towards this article, from data collection and analysis to writing and submission, were insightful and thought-provoking processes. We had a fantastic group of co-authors who made this body of work possible, despite being spread throughout multiple cities over a number of continents during the pandemic lockdown! The COVID-19 pandemic is something that touched nearly every human on planet Earth in some form, a reason why we strived to produce this publication, and why we hope you find our article an interesting and engaging read.
Ali Ebrahim
Read the Original
This page is a summary of: The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro), IUCrJ, August 2022, International Union of Crystallography,
DOI: 10.1107/s2052252522007497.
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