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
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

Auteurs

Maxim Stolyarchuk (M)

Centre Borelli, ENS Paris-Saclay, CNRS, Université Paris-Saclay, 4 Avenue des Sciences, 91190 Gif-sur-Yvette, France.

Marina Botnari (M)

Centre Borelli, ENS Paris-Saclay, CNRS, Université Paris-Saclay, 4 Avenue des Sciences, 91190 Gif-sur-Yvette, France.

Luba Tchertanov (L)

Centre Borelli, ENS Paris-Saclay, CNRS, Université Paris-Saclay, 4 Avenue des Sciences, 91190 Gif-sur-Yvette, France.

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Classifications MeSH