Structure, function and therapeutic implications of OB-fold proteins: A lesson from past to present.

OB-fold proteins genome stability single-stranded DNA-binding proteins telomere therapeutic intervention

Journal

Briefings in functional genomics
ISSN: 2041-2657
Titre abrégé: Brief Funct Genomics
Pays: England
ID NLM: 101528229

Informations de publication

Date de publication:
04 12 2020
Historique:
pubmed: 13 5 2020
medline: 12 10 2021
entrez: 13 5 2020
Statut: ppublish

Résumé

Oligonucleotide/oligosaccharide-binding (OB)-fold proteins play essential roles in the regulation of genome and its correct transformation to the subsequent generation. To maintain the genomic stability, OB-fold proteins are implicated in various cellular processes including DNA replication, DNA repair, cell cycle regulation and maintenance of telomere. The diverse functional spectrums of OB-fold proteins are mainly due to their involvement in protein-DNA and protein-protein complexes. Mutations and consequential structural alteration in the OB-fold proteins often lead to severe diseases. Here, we have investigated the structure, function and mode of action of OB-fold proteins (RPA, BRCA2, DNA ligases and SSBs1/2) in cellular pathways and their relationship with diseases and their possible use in therapeutic intervention. Due to the crucial role of OB-fold proteins in regulating the key physiological process, a detailed structural understanding in the context of underlying mechanism of action and cellular complexity offers a new avenue to target OB-proteins for therapeutic intervention.

Identifiants

pubmed: 32393969
pii: 5835911
doi: 10.1093/bfgp/elaa008
doi:

Substances chimiques

Carrier Proteins 0
Oligonucleotides 0
Telomere-Binding Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

377-389

Informations de copyright

© The Author(s) 2020. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com.

Auteurs

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Classifications MeSH