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3sfh

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<StructureSection load='3sfh' size='340' side='right'caption='[[3sfh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='3sfh' size='340' side='right'caption='[[3sfh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sfh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sfh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SFH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1DI:(2R)-2-AMINO-3-(2,4-DICHLOROPHENYL)-1-(1,3-DIHYDRO-2H-ISOINDOL-2-YL)PROPAN-1-ONE'>1DI</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sff|3sff]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1DI:(2R)-2-AMINO-3-(2,4-DICHLOROPHENYL)-1-(1,3-DIHYDRO-2H-ISOINDOL-2-YL)PROPAN-1-ONE'>1DI</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1, CDA07 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3sfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfh OCA], [https://pdbe.org/3sfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sfh RCSB], [https://www.ebi.ac.uk/pdbsum/3sfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sfh ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sfh OCA], [https://pdbe.org/3sfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sfh RCSB], [https://www.ebi.ac.uk/pdbsum/3sfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sfh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
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[https://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Herein we report the discovery of a family of novel yet simple, amino-acid derived class I HDAC inhibitors that demonstrate isoform selectivity via access to the internal acetate release channel. Isoform selectivity criteria is discussed on the basis of X-ray crystallography and molecular modeling of these novel inhibitors bound to HDAC8, potentially revealing insights into the mechanism of enzymatic function through novel structural features revealed at the atomic level.
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Human HDAC isoform selectivity achieved via exploitation of the acetate release channel with structurally unique small molecule inhibitors.,Whitehead L, Dobler MR, Radetich B, Zhu Y, Atadja PW, Claiborne T, Grob JE, McRiner A, Pancost MR, Patnaik A, Shao W, Shultz M, Tichkule R, Tommasi RA, Vash B, Wang P, Stams T Bioorg Med Chem. 2011 Aug 1;19(15):4626-34. Epub 2011 Jun 15. PMID:21723733<ref>PMID:21723733</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sfh" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Histone deacetylase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Stams, T]]
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[[Category: Stams T]]
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[[Category: Vash, B]]
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[[Category: Vash B]]
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[[Category: Deacetylase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]
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Current revision

Crystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived Inhibitor

PDB ID 3sfh

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