Modus operandi: Chromatin recognition by α-helical histone readers.
Structure
; 32(1): 8-17, 2024 01 04.
Article
em En
| MEDLINE
| ID: mdl-37922903
ABSTRACT
Histone reader domains provide a mechanism for sensing states of coordinated nuclear processes marked by histone proteins' post-translational modifications (PTMs). Among a growing number of discovered histone readers, the 14-3-3s, ankyrin repeat domains (ARDs), tetratricopeptide repeats (TPRs), bromodomains (BRDs), and HEAT domains are a group of domains using various mechanisms to recognize unmodified or modified histones, yet they all are composed of an α-helical fold. In this review, we compare how these readers fold to create protein domains that are very diverse in their tertiary structures, giving rise to intriguing peptide binding mechanisms resulting in vastly different footprints of their targets.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cromatina
/
Histonas
Idioma:
En
Revista:
Structure
Ano de publicação:
2024
Tipo de documento:
Article