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[[ | ==Crystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived Inhibitor== | ||
<StructureSection load='3sff' size='340' side='right' caption='[[3sff]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3sff]] is a 1 chain structure with sequence 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=3SFF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SFF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0DI:(2R)-2-AMINO-3-(3-CHLOROPHENYL)-1-[4-(2,5-DIFLUOROBENZOYL)PIPERAZIN-1-YL]PROPAN-1-ONE'>0DI</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sfh|3sfh]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC8, HDACL1, CDA07 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |||
<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> | |||
<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=3sff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sff OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sff RCSB], [http://www.ebi.ac.uk/pdbsum/3sff PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Histone deacetylase|Histone deacetylase]] | *[[Histone deacetylase|Histone deacetylase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Histone deacetylase]] | [[Category: Histone deacetylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Stams, T | [[Category: Stams, T]] | ||
[[Category: Vash, B | [[Category: Vash, B]] | ||
[[Category: Deacetylase]] | [[Category: Deacetylase]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
[[Category: Nvp-lci785]] | [[Category: Nvp-lci785]] | ||
Revision as of 16:34, 9 December 2014
Crystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived InhibitorCrystal Structure of Human HDAC8 Inhibitor Complex, an Amino Acid Derived Inhibitor
Structural highlights
Publication Abstract from PubMedHerein 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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