Article

D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes

2025-03-11

Abstract excerpt

The SARS-CoV-2 spike glycoprotein binds human epithelial cells and enables infection through a key conformational transition that exposes its receptor binding domain (RBD). Experimental evidence indicates that spike mutations, particularly the early D614G variant, alter the rate of this conformational shift, potentially increasing viral infectivity. To investigate how mutations reshape the conformational landscape...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 4a04d29a-a410-5c55-9096-a4dafcc2c1c8
DOI: 10.1101/2025.03.07.642081

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikesDOI 10.1101/2025.03.07.642081Read

D614G reshapes allosteric networks and opening mechanisms of SARS-CoV-2 spikes.Semantic proximity Read

Mutation and ACE2-induced Allosteric Network Rewiring in Delta and Omicron SARS-CoV-2 Spike ProteinsSemantic proximity Read

Structural Dynamics and Allosteric Communication of a SARS-Like Bat Coronavirus Spike GlycoproteinSemantic proximity Read

Structural dynamics and allosteric communication of a SARS-like bat coronavirus spike glycoprotein.Semantic proximity Read

The SARS-CoV-2 Spike Variant D614G Favors an Open Conformational StateSemantic proximity Read

Landscape-Based Protein Stability Analysis and Network Modeling of Multiple Conformational States of the SARS-CoV-2 Spike D614G Mutant: Conformational Plasticity and Frustration-Induced Allostery as Energetic Drivers of Highly Transmissible Spike Variants.Semantic proximity Read

Timeline of changes in spike conformational dynamics in emergent SARS-CoV-2 variants reveal progressive stabilization of trimer stalk with altered NTD dynamicsSemantic proximity Read

Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein.Semantic proximity Read

Allosteric Cross-Talk Among SARS-CoV-2 Spike’s Receptor-Binding Domain Mutations Triggers an Effective Hijacking of Human Cell ReceptorSemantic proximity Read

Structural Ramifications of Spike Protein D614G Mutation in SARS-CoV-2Semantic proximity Read

Omicron mutations increase interdomain interactions and reduce epitope exposure in the SARS-CoV-2 spikeSemantic proximity Read

Computational analysis of protein stability and allosteric interaction networks in distinct conformational forms of the SARS-CoV-2 spike D614G mutant: reconciling functional mechanisms through allosteric model of spike regulation.Semantic proximity Read