Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor.

Journal of molecular biology - 30 Dec 2022

Kovalevsky Andrey, Coates Leighton, Kneller Daniel W, Ghirlando Rodolfo, Aniana Annie, Nashed Nashaat T, Louis John M

Abstract excerpt

We recently demonstrated that inhibitor binding reorganizes the oxyanion loop of a monomeric catalytic domain of SARS CoV-2 main protease (MPro) from an unwound (E) to a wound (active, E*) conformation, independent of dimerization. Here we assess the effect of the flanking N-terminal residues, to imitate the MPro precursor prior to its autoprocessing, on conformational equilibria rendering stability and inhibitor...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalytic Domain
Share to Coronavirus 3C Proteases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Mutation

Share to Protein Stability

Share to SARS-CoV-2

Source

Open in PubMed Open full text

Identifiers

PMID: 36334779
DOI: 10.1016/j.jmb.2022.167876
PMCID: PMC9628131

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Unmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor.PMID 36334779Read ↗

Visualizing the Active Site Oxyanion Loop Transition Upon Ensitrelvir Binding and Transient Dimerization of SARS-CoV-2 Main Protease.Semantic proximity Read ↗

Cleavage at the nsp5-nsp6 site of SARS-CoV-2 main protease intermediate precursor is faster from a monomer than a dimer form.Semantic proximity Read ↗

Effects of SARS-CoV-2 Main Protease Mutations at Positions L50, E166, and L167 Rendering Resistance to Covalent and Noncovalent Inhibitors.Semantic proximity Read ↗

Mechanistic Insights into the Mutational Landscape of the Main Protease/3CLPro and Its Impact on Long-Term COVID-19/SARS-CoV-2 ManagementSemantic proximity Read ↗

SARS-CoV-2 main protease (M-pro) mutational profiling: An insight into mutation coldspots.Semantic proximity Read ↗

Identification of mutation resistance coldspots for targeting the SARS-CoV2 main protease.Semantic proximity Read ↗

Structures of Two Coronavirus Main Proteases: Implications for Substrate Binding and Antiviral Drug DesignSemantic proximity Read ↗

Autocatalytic maturation, physical/chemical properties, and crystal structure of group N HIV-1 protease: relevance to drug resistance.Semantic proximity Read ↗

Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site.Semantic proximity Read ↗

Interface design of SARS-CoV-2 symmetrical nsp7 dimer and machine learning-guided nsp7 sequence prediction reveals physicochemical properties and hotspots for nsp7 stability, adaptation, and therapeutic design.Semantic proximity Read ↗

Mechanism for controlling the monomer-dimer conversion of SARS coronavirus main protease.Semantic proximity Read ↗

Dynamical Nonequilibrium Molecular Dynamics Simulations Identify Allosteric Sites and Positions Associated with Drug Resistance in the SARS-CoV-2 Main ProteaseSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.