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Protein J . An Overview of the Crystallized Structures of the SARS-CoV-2

tetano

Editor, Senior Moderator
Protein J


. 2020 Oct 24.
doi: 10.1007/s10930-020-09933-w. Online ahead of print.
An Overview of the Crystallized Structures of the SARS-CoV-2


Mihaela Ileana Ionescu[SUP] 1 2 [/SUP]



Affiliations

Abstract

Many research teams all over the world focus their research on the SARS-CoV-2, the new coronavirus that causes the so-called COVID-19 disease. Most of the studies identify the main protease or 3C-like protease (M[SUP]pro[/SUP]/3CL[SUP]pro[/SUP]) as a valid target for large-spectrum inhibitors. Also, the interaction of the human receptor angiotensin-converting enzyme 2 (ACE2) with the viral surface glycoprotein (S) is studied in depth. Structural studies tried to identify the residues responsible for enhancement/weaken virus-ACE2 interactions or the cross-reactivity of the neutralizing antibodies. Although the understanding of the immune system and the hyper-inflammatory process in COVID-19 are crucial for managing the immediate and the long-term consequences of the disease, not many X-ray/NMR/cryo-EM crystals are available. In addition to 3CL[SUP]pro[/SUP], the crystal structures of other nonstructural proteins offer valuable information for elucidating some aspects of the SARS-CoV-2 infection. Thus, the structural analysis of the SARS-CoV-2 is currently mainly focused on three directions-finding M[SUP]pro[/SUP]/3CL[SUP]pro[/SUP] inhibitors, the virus-host cell invasion, and the virus-neutralizing antibody interaction.

Keywords: COVID-19; Coronavirus; Inhibitors; Molecular docking; Protein Data Bank; Spike.
 
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