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Article

Conformational dynamics of SARS-CoV-2 spike on a membrane reveals the allosteric effects of furin cleavage and the D614G mutation.

Science advances - 20 Mar 2026

Shoemaker Sophie R, Luo Megan, Dam Kim-Marie A, Pak John E, Hoffmann Magnus A G, Marqusee Susan

Abstract excerpt

By combining hydrogen-deuterium exchange monitored by mass spectrometry (HDX-MS) with the ability of enveloped virus-like particles (eVLPs) to display full-length native-like severe acute respiratory syndrome coronavirus 2 spike protein, we have determined the energetic and conformational effects of both the membrane environment and unique sequence features that are considered incompatible with soluble protein...

Topics

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Allosteric Regulation
Cell Membrane
Furin
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Serine Endopeptidases

Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 41861002
DOI: 10.1126/sciadv.adx5178
PMCID: PMC13004018

Genes

HDX
TMPRSS2

Provenance

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

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