Vitamin K Epoxide Reductase Complex-Protein Disulphide Isomerase Assemblies in the Thiol-Disulphide Exchange Reactions: Portrayal of Precursor-to-Successor Complexes.
3D modelling
PDI–hVKORC1
allosteric regulation
computational biophysics
intrinsic disorder
molecular dynamics
molecular interactions
precursor, intermediate, and successor complexes
protein folding
thiol–disulphide exchange reactions
transient states
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
09 Apr 2024
09 Apr 2024
Historique:
received:
06
03
2024
revised:
04
04
2024
accepted:
05
04
2024
medline:
27
4
2024
pubmed:
27
4
2024
entrez:
27
4
2024
Statut:
epublish
Résumé
The human Vitamin K Epoxide Reductase Complex (hVKORC1), a key enzyme that converts vitamin K into the form necessary for blood clotting, requires for its activation the reducing equivalents supplied by its redox partner through thiol-disulphide exchange reactions. The functionally related molecular complexes assembled during this process have never been described, except for a proposed de novo model of a 'precursor' complex of hVKORC1 associated with protein disulphide isomerase (PDI). Using numerical approaches (
Identifiants
pubmed: 38673722
pii: ijms25084135
doi: 10.3390/ijms25084135
pii:
doi:
Substances chimiques
Protein Disulfide-Isomerases
EC 5.3.4.1
Vitamin K Epoxide Reductases
EC 1.17.4.4
Disulfides
0
Sulfhydryl Compounds
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM