Intrinsically disordered proteins in viral pathogenesis and infections.
Adv Protein Chem Struct Biol
; 132: 221-242, 2022.
Artículo
en Inglés
| MEDLINE | ID: covidwho-2003777
ABSTRACT
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.
Palabras clave
Texto completo:
Disponible
Colección:
Bases de datos internacionales
Base de datos:
MEDLINE
Asunto principal:
Proteínas Intrínsecamente Desordenadas
Idioma:
Inglés
Revista:
Adv Protein Chem Struct Biol
Asunto de la revista:
Biologia
/
Bioquímica
Año:
2022
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS