5zoo

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'''Unreleased structure'''
 
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The entry 5zoo is ON HOLD until Apr 13 2020
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==Crystal structure of histone deacetylase 4 (HDAC4) in complex with a SMRT corepressor SP1 fragment==
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<StructureSection load='5zoo' size='340' side='right' caption='[[5zoo]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5zoo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZOO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZOO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.98 3.5.1.98] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zoo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zoo OCA], [http://pdbe.org/5zoo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zoo RCSB], [http://www.ebi.ac.uk/pdbsum/5zoo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zoo ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/HDAC4_HUMAN HDAC4_HUMAN]] Defects in HDAC4 are the cause of brachydactyly-mental retardation syndrome (BDMR) [MIM:[http://omim.org/entry/600430 600430]]. A syndrome resembling the physical anomalies found in Albright hereditary osteodystrophy. Common features are mild facial dysmorphism, congenital heart defects, distinct brachydactyly type E, mental retardation, developmental delay, seizures, autism spectrum disorder, and stocky build. Soft tissue ossification is absent, and there are no abnormalities in parathyroid hormone or calcium metabolism.<ref>PMID:20691407</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/HDAC4_HUMAN HDAC4_HUMAN]] Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D.<ref>PMID:10523670</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Modification of chromatin and related transcription factors by histone deacetylases (HDACs) is one of the major strategies for controlling gene expression in eukaryotes. The HDAC domains of class IIa HDACs repress the respective target genes by interacting with the C-terminal region of the silencing mediator for retinoid and thyroid receptor (SMRT) repression domain 3 (SRD3c). However, latent catalytic activity suggests that their roles as deacetylases in gene regulation are unclear. Here, we found that two conserved GSI-containing motifs of SRD3c are critical for HDAC4 binding. Two SMRT peptides including these motifs commonly form a beta-hairpin structure in the cleft and block the catalytic entry site of HDAC4. They interact mainly with class IIa HDAC-specific residues of HDAC4 in a closed conformation. Structure-guided mutagenesis confirmed critical interactions between the SMRT peptides and HDAC4 and -5 as well as the contribution of the Arg1369 residue in the first motif for optimal binding to the two HDACs. These results indicate that SMRT binding does not activate the cryptic deacetylase activity of HDAC4 and explain how class IIa HDACs and the SMRT-HDAC3 complex are coordinated during gene regulation.
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Authors: Park, S.Y., Hwang, H.J., Kim, J.S.
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Structural basis of the specific interaction of SMRT corepressor with histone deacetylase 4.,Park SY, Kim GS, Hwang HJ, Nam TH, Park HS, Song J, Jang TH, Lee YC, Kim JS Nucleic Acids Res. 2018 Oct 13. pii: 5128926. doi: 10.1093/nar/gky926. PMID:30321390<ref>PMID:30321390</ref>
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Description: Crystal structure of histone deacetylase 4 (HDAC4) in complex with a SMRT corepressor SP1 fragment
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kim, J.S]]
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<div class="pdbe-citations 5zoo" style="background-color:#fffaf0;"></div>
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[[Category: Park, S.Y]]
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== References ==
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[[Category: Hwang, H.J]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Histone deacetylase]]
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[[Category: Hwang, H J]]
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[[Category: Kim, J S]]
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[[Category: Park, S Y]]
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[[Category: Hydrolase]]
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[[Category: Protein-peptide complex]]

Revision as of 08:05, 14 November 2018

Crystal structure of histone deacetylase 4 (HDAC4) in complex with a SMRT corepressor SP1 fragment

5zoo, resolution 1.85Å

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