An Overview of the Crystallized Structures of the SARS-CoV-2. Protein J 2020 Dec;39(6):600-618
Date
10/25/2020Pubmed ID
33098476Pubmed Central ID
PMC7584483DOI
10.1007/s10930-020-09933-wScopus ID
2-s2.0-85093922788 (requires institutional sign-in at Scopus site) 33 CitationsAbstract
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 (Mpro/3CLpro) 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 3CLpro, 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 Mpro/3CLpro inhibitors, the virus-host cell invasion, and the virus-neutralizing antibody interaction.
Author List
Ionescu MIAuthor
Deborah M. Costakos MD Chair, Professor in the Ophthalmology and Visual Sciences department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAntiviral Agents
Cryoelectron Microscopy
Crystallography, X-Ray
Drug Discovery
Humans
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular
Phosphoproteins
Protein Conformation
Protein Kinase Inhibitors
