1n6j
From Proteopedia
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Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2
Overview
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.
About this Structure
1N6J is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Sequence-specific recruitment of transcriptional co-repressor Cabin1 by myocyte enhancer factor-2., Han A, Pan F, Stroud JC, Youn HD, Liu JO, Chen L, Nature. 2003 Apr 17;422(6933):730-4. PMID:12700764
Page seeded by OCA on Mon Nov 12 18:18:12 2007
