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
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
377-389Informations de copyright
© The Author(s) 2020. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com.