Conformational Control of Fast Asparagine Deamidation in a Norovirus Capsid Protein.
Journal
Biochemistry
ISSN: 1520-4995
Titre abrégé: Biochemistry
Pays: United States
ID NLM: 0370623
Informations de publication
Date de publication:
07 03 2023
07 03 2023
Historique:
pubmed:
23
2
2023
medline:
9
3
2023
entrez:
22
2
2023
Statut:
ppublish
Résumé
Accelerated spontaneous deamidation of asparagine 373 and subsequent conversion into an isoaspartate has been shown to attenuate the binding of histo blood group antigens (HBGAs) to the protruding domain (P-domain) of the capsid protein of a prevalent norovirus strain (GII.4). Here, we link an unusual backbone conformation of asparagine 373 to its fast site-specific deamidation. NMR spectroscopy and ion exchange chromatography have been used to monitor the deamidation reaction of P-domains of two closely related GII.4 norovirus strains, specific point mutants, and control peptides. MD simulations over several microseconds have been instrumental to rationalize the experimental findings. While conventional descriptors such as available surface area, root-mean-square fluctuations, or nucleophilic attack distance fail as explanations, the population of a rare
Identifiants
pubmed: 36808948
doi: 10.1021/acs.biochem.2c00656
pmc: PMC9996831
doi:
Substances chimiques
Capsid Proteins
0
Asparagine
7006-34-0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1032-1043Références
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