6C9L

MEF2B Apo Protein Structure

Summary for 6C9L

• Entry DOI: 10.2210/pdb6c9l/pdb
• Descriptor: Myocyte-specific enhancer factor 2B (2 entities in total)
• Functional Keywords: mef2, mef2b, mef2b apo structure, self-regulatory protein, transcription
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 6
• Total formula weight: 66233.13

Authors

Lei, X.,Chen, L. (deposition date: 2018-01-26, release date: 2018-02-07, Last modification date: 2024-03-13)

Primary citation

Lei, X.,Shi, H.,Kou, Y.,Rajashekar, N.,Wu, F.,Sen, C.,Xu, J.,Chen, L.
Crystal Structure of Apo MEF2B Reveals New Insights in DNA Binding and Cofactor Interaction.
Biochemistry, 57:4047-4051, 2018

PubMed Abstract: The myocyte enhancer factor 2 (MEF2) family of transcription factors plays important roles in developmental processes and adaptive responses. Although MEF2 proteins are known to bind DNA in the nucleus to regulate specific gene expression, there are reports that show that MEF2 also functions in the cytoplasm. Previous structural studies of MEF2 focused exclusively on DNA-bound MEF2 with and without various corepressors or coactivators. While these studies have established a comprehensive structural model of DNA recognition and cofactor recruitment by MEF2, the structure of MEF2 not bound to DNA, which include cytoplasmic MEF2 and free MEF2 in the nucleus, is unknown. Here we determined the structure of the MADS-box/MEF2 domain of MEF2B without DNA nor cofactor. The Apo structure of MEF2B reveals a largely preformed DNA binding interface that may be important for recognizing the shape of DNA from the minor groove side. In addition, our structure also reveals that the C-terminal helix of the MEF2-specific domain could flip up to bind to the hydrophobic groove that serves as the binding sites of MEF2 transcription cofactors. These observations shed new insights into DNA binding and cofactor interaction by MEF2 proteins.

PubMed: 29944822
DOI: 10.1021/acs.biochem.8b00439

Experimental method

X-RAY DIFFRACTION (2.3 Å)