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Article

The allosteric switching mechanism in bacteriophage MS2.

The Journal of chemical physics - 21 Jul 2016

Perkett Matthew R, Mirijanian Dina T, Hagan Michael F

Abstract excerpt

We use all-atom simulations to elucidate the mechanisms underlying conformational switching and allostery within the coat protein of the bacteriophage MS2. Assembly of most icosahedral virus capsids requires that the capsid protein adopts different conformations at precise locations within the capsid. It has been shown that a 19 nucleotide stem loop (TR) from the MS2 genome acts as an allosteric effector, guiding...

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Identifiers

PMID: 27448905
DOI: 10.1063/1.4955187
PMCID: PMC4947040

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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