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

Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro.

Communications biology - 2 May 2026

Creon Anne, Scheer T Emilie S, Reinke Patrick, Rahmani Mashhour Aida, Günther Sebastian, Niebling Stephan, Schamoni-Kast Kira, Uetrecht Charlotte, Meents Alke, Chapman Henry N, Sprenger Janina, Lane Thomas J

Abstract excerpt

To interpret and transmit biological signals, proteins use correlated motions. Experimental determination of these dynamics and the structural distributions they generate remains a key challenge. Here, using 1146 crystal structures of the main protease (Mpro) from SARS-CoV-2, we were able to infer a model of the enzyme's structural fluctuations. Mpro is regulated by concentration, becoming enzymatically active...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Regulation
Share to Betacoronavirus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalytic Domain

Share to Coronavirus 3C Proteases

Share to Crystallography, X-Ray

Share to Protein Multimerization

Share to SARS-CoV-2

Share to Viral Nonstructural Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 42069849
DOI: 10.1038/s42003-026-10127-w
PMCID: PMC13135515

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Statistical crystallography reveals an allosteric network in SARS-CoV-2 Mpro.PMID 42069849Read ↗

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

SARS-CoV-2 main protease mutation analysis via a kinematic method.Semantic proximity Read ↗

Mutation-Induced Resistance of SARS-CoV-2 Mpro to WU-04 Revealed by Multi-Scale Modeling.Semantic proximity Read ↗

Impact of Early Pandemic Stage Mutations on Molecular Dynamics of SARS-CoV-2 Mpro.Semantic proximity Read ↗

Molecular insights from conformational ensembles via machine learningSemantic proximity Read ↗

Dynamic Profiling of β-Coronavirus 3CL Mpro Protease Ligand-Binding SitesSemantic proximity Read ↗

Mutation Effects on Structure and Dynamics: Adaptive Evolution of the SARS-CoV-2 Main Protease.Semantic proximity Read ↗

Evolution of the SARS-CoV-2 main protease under fitness constraints imposed by folding stability and activitySemantic proximity Read ↗

Computational Analysis of Dynamic Allostery and Control in the three SARS-CoV-2 non-structural proteinsSemantic proximity Read ↗

Cooperativity and communication between the active sites of the dimeric SARS-CoV-2 main protease.Semantic proximity Read ↗

PLANET-MD: Ultra-fast Proteome-scale Prediction of Allosteric Networks in ProteinsSemantic proximity Read ↗

Allosteric Regulation of SARS-CoV-2 Protease: Towards Informed Structure-Based Drug DiscoverySemantic proximity Read ↗

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