1N6J: Structural Basis of Sequence-specific Recruitment of Histone Deacetylases by Myocyte Enhancer Factor-2

Citation:
Abstract
The myocyte enhancer factor-2 (MEF2) family of transcription factors has important roles in the development and function of T cells, neuronal cells and muscle cells. MEF2 is capable of repressing or activating transcription by association with a variety of co-repressors or co-activators in a calcium-dependent manner. Transcriptional repression by MEF2 has attracted particular attention because of its potential role in hypertrophic responses of cardiomyocytes. Several MEF2 co-repressors, such as Cabin1/Cain and class II histone deacetylases (HDACs), have been identified. However, the molecular mechanism of their recruitment to specific promoters by MEF2 remains largely unknown. Here we report a crystal structure of the MADS-box/MEF2S domain of human MEF2B bound to a motif of the transcriptional co-repressor Cabin1 and DNA at 2.2 A resolution. The crystal structure reveals a stably folded MEF2S domain on the surface of the MADS box. Cabin1 adopts an amphipathic alpha-helix to bind a hydrophobic groove on the MEF2S domain, forming a triple-helical interaction. Our studies of the ternary Cabin1/MEF2/DNA complex show a general mechanism by which MEF2 recruits transcriptional co-repressor Cabin1 and class II HDACs to specific DNA sites.
PDB ID: 1N6JDownload
MMDB ID: 74075
PDB Deposition Date: 2002/11/11
Updated in MMDB: 2015/09 
Experimental Method:
x-ray diffraction
Resolution: 2.2  Å
Similar Structures:
Biological Unit for 1N6J: pentameric; determined by author
Molecular Components in 1N6J
Label Count Molecule
Proteins (3 molecules)
2
Myocyte-specific Enhancer Factor 2B
Molecule annotation
1
Calcineurin-binding Protein Cabin 1
Molecule annotation
Nucleotides(2 molecules)
1
5'-d(*ap*gp*cp*tp*ap*tp*tp*tp*ap*tp*ap*ap*gp*c)-3'
Molecule annotation
1
5'-d(*gp*cp*tp*tp*ap*tp*ap*ap*ap*tp*ap*gp*cp*t)-3'
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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