1n6j: Difference between revisions

Revision as of 12:38, 10 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n6j.png

Template:STRUCTURE 1n6j

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

Template:ABSTRACT PUBMED 12700764

About this StructureAbout this Structure

1N6J is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-'''Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2'''
+===Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2===
-==Overview==
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-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.
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 ==About this Structure==
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 [[Category: Mads-box]]
 [[Category: Protein-dna complex]]
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