1n6j
From Proteopedia
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|PDB= 1n6j |SIZE=350|CAPTION= <scene name='initialview01'>1n6j</scene>, resolution 2.20Å | |PDB= 1n6j |SIZE=350|CAPTION= <scene name='initialview01'>1n6j</scene>, resolution 2.20Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= MEF2B OR XMEF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CABIN1 OR KIAA0330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= MEF2B OR XMEF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), CABIN1 OR KIAA0330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n6j OCA], [http://www.ebi.ac.uk/pdbsum/1n6j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n6j RCSB]</span> | ||
}} | }} | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:26:03 2008'' |
Revision as of 19:26, 30 March 2008
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, resolution 2.20Å | |||||||
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Ligands: | , , , | ||||||
Gene: | MEF2B OR XMEF2 (Homo sapiens), CABIN1 OR KIAA0330 (Homo sapiens) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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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