Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification.
Biocomputational method
Biomolecules
Electrostatics
Glutaredoxin
Gromov-Wasserstein distance
Mathematical biosciences
Molecular docking
Protein-protein interaction
Redox signaling
Thioredoxin
Journal
Heliyon
ISSN: 2405-8440
Titre abrégé: Heliyon
Pays: England
ID NLM: 101672560
Informations de publication
Date de publication:
Dec 2019
Dec 2019
Historique:
received:
22
05
2019
revised:
15
11
2019
accepted:
25
11
2019
entrez:
1
1
2020
pubmed:
1
1
2020
medline:
1
1
2020
Statut:
epublish
Résumé
The spatio-temporal reduction and oxidation of protein thiols is an essential mechanism in signal transduction in all kingdoms of life. Thioredoxin (Trx) family proteins efficiently catalyze thiol-disulfide exchange reactions and the proteins are widely recognized for their importance in the operation of thiol switches. Trx family proteins have a broad and at the same time very distinct substrate specificity - a prerequisite for redox switching. Despite of multiple efforts, the true nature for this specificity is still under debate. Here, we comprehensively compare the classification/clustering of various redoxins from all domains of life based on their similarity in amino acid sequence, tertiary structure, and their electrostatic properties. We correlate these similarities to the existence of common interaction partners, identified in various previous studies and suggested by proteomic screenings. These analyses confirm that primary and tertiary structure similarity, and thereby all common classification systems, do not correlate to the target specificity of the proteins as thiol-disulfide oxidoreductases. Instead, a number of examples clearly demonstrate the importance of electrostatic similarity for their target specificity, independent of their belonging to the Trx or glutaredoxin subfamilies.
Identifiants
pubmed: 31890941
doi: 10.1016/j.heliyon.2019.e02943
pii: S2405-8440(19)36602-2
pii: e02943
pmc: PMC6928294
doi:
Types de publication
Journal Article
Langues
eng
Pagination
e02943Informations de copyright
© 2019 The Author(s).
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