1N6J

Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2

Summary for 1N6J

• Entry DOI: 10.2210/pdb1n6j/pdb
• Descriptor: 5'-D(*AP*GP*CP*TP*AP*TP*TP*TP*AP*TP*AP*AP*GP*C)-3', 5'-D(*GP*CP*TP*TP*AP*TP*AP*AP*AP*TP*AP*GP*CP*T)-3', Myocyte-specific enhancer factor 2B, ... (5 entities in total)
• Functional Keywords: mads-box, protein-dna complex, histone deacetylases, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q02080 Q9Y6J0
• Total number of polymer chains: 5
• Total formula weight: 34207.33

Authors

Han, A.,Pan, F.,Stroud, J.C.,Youn, H.D.,Liu, J.O.,Chen, L. (deposition date: 2002-11-11, release date: 2003-11-11, Last modification date: 2024-02-14)

Primary citation

Han, A.,Pan, F.,Stroud, J.C.,Youn, H.D.,Liu, J.O.,Chen, L.
Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2
Nature, 422:730-734, 2003

PubMed 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.

PubMed: 12700764
DOI: 10.1038/nature01555

Experimental method

X-RAY DIFFRACTION (2.2 Å)