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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 12 May 2026

Kearns Fiona L, Bogetti Anthony T, Calvó-Tusell Carla, Braza Mac Kevin E, Casalino Lorenzo, Gramm Amanda J, Braet Sean, Rosenfeld Mia A, Rajapaksha Harinda, Barker Bryan, Anand Ganesh, Chong Lillian T, Ahn Surl-Hee, Amaro Rommie E

Abstract excerpt

The severe acute respiratory syndrome coronavirus 2 spike glycoprotein 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. We conducted extensive weighted ensemble simulations of the...

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Allosteric Regulation
Binding Sites
COVID-19
Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Protein Domains

Spike Glycoprotein, Coronavirus

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Identifiers

PMID: 42101997
DOI: 10.1073/pnas.2504793123
PMCID: PMC13168548

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

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