8g44
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Structure of HDAC6 zinc-finger ubiquitin binding domain in complex with 3-(3-(2-(benzylamino)-2-oxoethyl)-4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid== | |
- | + | <StructureSection load='8g44' size='340' side='right'caption='[[8g44]], [[Resolution|resolution]] 1.55Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8g44]] 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=8G44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8G44 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ZU9:3-{3-[2-(benzylamino)-2-oxoethyl]-4-oxo-3,4-dihydroquinazolin-2-yl}propanoic+acid'>ZU9</scene></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=8g44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8g44 OCA], [https://pdbe.org/8g44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8g44 RCSB], [https://www.ebi.ac.uk/pdbsum/8g44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8g44 ProSAT]</span></td></tr> |
- | [[ | + | </table> |
- | [[ | + | == Function == |
- | [[Category: | + | [https://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> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Homo sapiens]] |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: | + | [[Category: Ackloo S]] |
- | [[Category: | + | [[Category: Arrowsmith CH]] |
- | [[Category: | + | [[Category: Baker RJ]] |
- | [[Category: | + | [[Category: Barsyte-Lovejoy D]] |
- | [[Category: | + | [[Category: Brown PJ]] |
- | [[Category: | + | [[Category: Dank C]] |
- | [[Category: Mirabi | + | [[Category: Franzoni I]] |
- | [[Category: | + | [[Category: Harding RJ]] |
- | [[Category: | + | [[Category: Juarez-Ornelas KA]] |
- | [[Category: | + | [[Category: Lautens M]] |
+ | [[Category: Mann MK]] | ||
+ | [[Category: Mirabi B]] | ||
+ | [[Category: Owens DDG]] | ||
+ | [[Category: Sanichar R]] | ||
+ | [[Category: Santhakumar V]] | ||
+ | [[Category: Schapira M]] | ||
+ | [[Category: Scheremetjew A]] | ||
+ | [[Category: Szewczyk M]] |
Revision as of 07:31, 3 May 2023
Structure of HDAC6 zinc-finger ubiquitin binding domain in complex with 3-(3-(2-(benzylamino)-2-oxoethyl)-4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
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Categories: Homo sapiens | Large Structures | Ackloo S | Arrowsmith CH | Baker RJ | Barsyte-Lovejoy D | Brown PJ | Dank C | Franzoni I | Harding RJ | Juarez-Ornelas KA | Lautens M | Mann MK | Mirabi B | Owens DDG | Sanichar R | Santhakumar V | Schapira M | Scheremetjew A | Szewczyk M