1tqe

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Revision as of 17:20, 12 November 2007

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spinqualitylabelsall models 1tqe, resolution 2.7Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2

Overview

Class II histone deacetylases (HDACs) bind myocyte enhancer factor-2, (MEF2) and repress specific gene expression in a calcium-dependent manner., Despite their significant physiological functions in muscle, immune and, neuronal cells, the mechanism of recruitment of class II HDACs by MEF2 is, not well understood. Here, we have characterized the complex between the, MEF2-binding motif of class II HDACs and the MADS-box/MEF2S domain of, MEF2B by structural and biochemical methods. The crystal structure of a, HDAC9/MEF2/DNA complex reveals that HDAC9 binds to a hydrophobic groove of, the MEF2 dimer. The overall binding mode is similar to that seen in the, Cabin1/MEF2/DNA complex. The detailed binding interactions at the, HDAC9/MEF2 interface, however, show marked differences from those at the, Cabin1/MEF2 interface. Our studies suggest a general mechanism by which, class II HDACs and possibly other transcriptional co-regulators are, recruited by MEF2. On the other hand, the differential binding between, MEF2 and its various partners may confer specific regulatory and, functional properties to MEF2 in distinct cellular processes. Such, specificity provides a basis for selectively disrupting a particular, MEF2/co-regulator complex by mutations or small molecules.

About this Structure

1TQE is a Protein complex structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.

Reference

Mechanism of recruitment of class II histone deacetylases by myocyte enhancer factor-2., Han A, He J, Wu Y, Liu JO, Chen L, J Mol Biol. 2005 Jan 7;345(1):91-102. PMID:15567413

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