5b8d: Difference between revisions

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'''Unreleased structure'''


The entry 5b8d is ON HOLD  until Sep 20 2017
==Crystal structure of a low occupancy fragment candidate (N-(4-Methyl-1,3-thiazol-2-yl)propanamide) bound adjacent to the ubiquitin binding pocket of the HDAC6 zinc-finger domain==
 
<StructureSection load='5b8d' size='340' side='right' caption='[[5b8d]], [[Resolution|resolution]] 1.05&Aring;' scene=''>
Authors: Harding, R.J., Tempel, W., Collins, P., Pearce, N., Brandao-Neto, J., Douangamath, A., Ravichandran, M., Schapira, M., Bountra, C., Edwards, A.M., von Delft, F., Santhakumar, V., Arrowsmith, C.M., Structural Genomics Consortium (SGC)
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5b8d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B8D FirstGlance]. <br>
Description: Crystal structure of a low occupancy fragment candidate (N-(4-Methyl-1,3-thiazol-2-yl)propanamide) bound adjacent to the ubiquitin binding pocket of the HDAC6 zinc-finger domain
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6T4:~{N}-(4-METHYL-1,3-THIAZOL-2-YL)ETHANAMIDE'>6T4</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5kh3|5kh3]], [[5kh7|5kh7]], [[5kh9|5kh9]]</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=5b8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b8d OCA], [http://pdbe.org/5b8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b8d RCSB], [http://www.ebi.ac.uk/pdbsum/5b8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b8d ProSAT]</span></td></tr>
</table>
== Function ==
[[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> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Histone deacetylase]]
[[Category: Arrowsmith, C M]]
[[Category: Bountra, C]]
[[Category: Brandao-Neto, J]]
[[Category: Collins, P]]
[[Category: Collins, P]]
[[Category: Brandao-Neto, J]]
[[Category: Delft, F von]]
[[Category: Douangamath, A]]
[[Category: Edwards, A M]]
[[Category: Harding, R J]]
[[Category: Pearce, N]]
[[Category: Ravichandran, M]]
[[Category: Structural genomic]]
[[Category: Santhakumar, V]]
[[Category: Santhakumar, V]]
[[Category: Ravichandran, M]]
[[Category: Arrowsmith, C.M]]
[[Category: Von Delft, F]]
[[Category: Pearce, N]]
[[Category: Schapira, M]]
[[Category: Schapira, M]]
[[Category: Edwards, A.M]]
[[Category: Structural Genomics Consortium (Sgc)]]
[[Category: Douangamath, A]]
[[Category: Harding, R.J]]
[[Category: Bountra, C]]
[[Category: Tempel, W]]
[[Category: Tempel, W]]
[[Category: Diamond i04-1 xchem]]
[[Category: Fragment screening]]
[[Category: Hdac]]
[[Category: Hdac6]]
[[Category: Hydrolase]]
[[Category: Pandda]]
[[Category: Sgc]]
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