Intrinsically disordered proteins in viral pathogenesis and infections.
Disorder proteins
Flavivirus
HIV-1
IDP
IDP servers
IPDs
Molecular dynamics
PONDR
Proteins
SARS-CoV-2
Viral proteome
Virulence
Virus
Journal
Advances in protein chemistry and structural biology
ISSN: 1876-1631
Titre abrégé: Adv Protein Chem Struct Biol
Pays: Netherlands
ID NLM: 101497281
Informations de publication
Date de publication:
2022
2022
Historique:
entrez:
10
9
2022
pubmed:
11
9
2022
medline:
14
9
2022
Statut:
ppublish
Résumé
Disordered proteins serve a crucial part in many biological processes that go beyond the capabilities of ordered proteins. A large number of virus-encoded proteins have extremely condensed proteomes and genomes, which results in highly disordered proteins. The presence of these IDPs allows them to rapidly adapt to changes in their biological environment and play a significant role in viral replication and down-regulation of host defense mechanisms. Since viruses undergo rapid evolution and have a high rate of mutation and accumulation in their proteome, IDPs' insights into viruses are critical for understanding how viruses hijack cells and cause disease. There are many conformational changes that IDPs can adopt in order to interact with different protein partners and thus stabilize the particular fold and withstand high mutation rates. This chapter explains the molecular mechanism behind viral IDPs, as well as the significance of recent research in the field of IDPs, with the goal of gaining a deeper comprehension of the essential roles and functions played by viral proteins.
Identifiants
pubmed: 36088077
pii: S1876-1623(22)00055-4
doi: 10.1016/bs.apcsb.2022.06.002
pii:
doi:
Substances chimiques
Intrinsically Disordered Proteins
0
Proteome
0
Viral Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
221-242Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.