5kh3

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'''Unreleased structure'''
 
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The entry 5kh3 is ON HOLD until Sep 20 2017
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==Crystal structure of fragment (3-(5-Chloro-1,3-benzothiazol-2-yl)propanoic acid) bound in the ubiquitin binding pocket of the HDAC6 zinc-finger domain==
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<StructureSection load='5kh3' size='340' side='right' caption='[[5kh3]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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Authors: Harding, R.J., Dong, A., Ravichandran, M., Schapira, M., Bountra, C., Edwards, A.M., Santhakumar, V., Arrowsmith, C.M., Structural Genomics Consortium (SGC)
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5kh3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KH3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KH3 FirstGlance]. <br>
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Description: Crystal structure of fragment (3-(5-Chloro-1,3-benzothiazol-2-yl)propanoic acid) bound in the ubiquitin binding pocket of the HDAC6 zinc-finger domain
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6U6:3-(5-CHLORANYL-1,3-BENZOTHIAZOL-2-YL)PROPANOIC+ACID'>6U6</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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[[Category: Unreleased Structures]]
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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=5kh3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kh3 OCA], [http://pdbe.org/5kh3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kh3 RCSB], [http://www.ebi.ac.uk/pdbsum/5kh3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kh3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/HDAC6_HUMAN HDAC6_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 (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin.<ref>PMID:12024216</ref> <ref>PMID:17846173</ref> In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.<ref>PMID:12024216</ref> <ref>PMID:17846173</ref>
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== References ==
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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: Arrowsmith, C M]]
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[[Category: Bountra, C]]
[[Category: Dong, A]]
[[Category: Dong, A]]
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[[Category: Edwards, A M]]
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[[Category: Freitas, R Ferreira de]]
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[[Category: Harding, R J]]
[[Category: Ravichandran, M]]
[[Category: Ravichandran, M]]
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[[Category: Arrowsmith, C.M]]
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[[Category: Structural genomic]]
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[[Category: Santhakumar, V]]
[[Category: Schapira, M]]
[[Category: Schapira, M]]
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[[Category: Bountra, C]]
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[[Category: Fragment screening]]
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[[Category: Santhakumar, V]]
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[[Category: Hdac]]
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[[Category: Edwards, A.M]]
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[[Category: Hdac6]]
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[[Category: Structural Genomics Consortium (Sgc)]]
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[[Category: Hydrolase]]
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[[Category: Harding, R.J]]
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[[Category: Sgc]]

Revision as of 15:47, 27 July 2016

Crystal structure of fragment (3-(5-Chloro-1,3-benzothiazol-2-yl)propanoic acid) bound in the ubiquitin binding pocket of the HDAC6 zinc-finger domain

5kh3, resolution 1.60Å

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