1n6j
From Proteopedia
(New page: 200px<br /> <applet load="1n6j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6j, resolution 2.20Å" /> '''Structural basis of...) |
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caption="1n6j, resolution 2.20Å" /> | caption="1n6j, resolution 2.20Å" /> | ||
'''Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2'''<br /> | '''Structural basis of sequence-specific recruitment of histone deacetylases by Myocyte Enhancer Factor-2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The myocyte enhancer factor-2 (MEF2) family of transcription factors has | + | 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== | ==About this Structure== | ||
| - | 1N6J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1N6J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N6J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Han, A.]] | [[Category: Han, A.]] | ||
| - | [[Category: Liu, J | + | [[Category: Liu, J O.]] |
[[Category: Pan, F.]] | [[Category: Pan, F.]] | ||
| - | [[Category: Stroud, J | + | [[Category: Stroud, J C.]] |
| - | [[Category: Youn, H | + | [[Category: Youn, H D.]] |
[[Category: histone deacetylases]] | [[Category: histone deacetylases]] | ||
[[Category: mads-box]] | [[Category: mads-box]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:46 2008'' |
Revision as of 12:02, 21 February 2008
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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
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