Structural basis of the bHLH domains of MyoD-E47 heterodimer.
Crystal structure
E47
Heterodimer
MyoD
bHLH domain
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
17 09 2022
17 09 2022
Historique:
received:
05
06
2022
revised:
15
06
2022
accepted:
22
06
2022
pubmed:
11
7
2022
medline:
6
8
2022
entrez:
10
7
2022
Statut:
ppublish
Résumé
The basic helix-loop-helix (bHLH) family is one of the most conserved transcription factor families that plays an important role in regulating cell growth, differentiation and tissue development. Typically, members of this family form homo- or heterodimers to recognize specific motifs and activate transcription. MyoD is a vital transcription factor that regulates muscle cell differentiation. However, it is necessary for MyoD to form a heterodimer with E-proteins to activate transcription. Even though the crystal structure of the MyoD homodimer has been determined, the structure of the MyoD heterodimer in complex with the E-box protein remains unclear. In this study, we determined the crystal structure of the bHLH domain of the MyoD-E47 heterodimer at 2.05 Å. Our structural analysis revealed that MyoD interacts with E47 through a hydrophobic interface. Moreover, we confirmed that heterodimerization could enhance the binding affinity of MyoD to E-box sequences. Our results provide new structural insights into the heterodimer of MyoD and E-box protein, suggesting the molecular mechanism of transcription activation of MyoD upon binding to E-box protein.
Identifiants
pubmed: 35810596
pii: S0006-291X(22)00925-1
doi: 10.1016/j.bbrc.2022.06.071
pii:
doi:
Substances chimiques
DNA-Binding Proteins
0
MyoD Protein
0
TCF Transcription Factors
0
Transcription Factor 7-Like 1 Protein
0
Transcription Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
88-93Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.