7WZ6

Crystal structure of MyoD-E47

Summary for 7WZ6

• Entry DOI: 10.2210/pdb7wz6/pdb
• Descriptor: Isoform E47 of Transcription factor E2-alpha, Myoblast determination protein 1 (3 entities in total)
• Functional Keywords: e-box, bhlh domain, transcription
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 2
• Total formula weight: 15748.23

Authors

Zhong, J.,Huang, Y.,Ma, J. (deposition date: 2022-02-17, release date: 2022-06-22, Last modification date: 2024-01-17)

Primary citation

Zhong, J.,Jin, Z.,Jiang, L.,Zhang, L.,Hu, Z.,Zhang, Y.,Liu, Y.,Ma, J.,Huang, Y.
Structural basis of the bHLH domains of MyoD-E47 heterodimer.
Biochem.Biophys.Res.Commun., 621:88-93, 2022

PubMed Abstract: 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.

PubMed: 35810596
DOI: 10.1016/j.bbrc.2022.06.071

Experimental method

X-RAY DIFFRACTION (2.05 Å)