3phd: Difference between revisions

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 ==Crystal structure of human HDAC6 in complex with ubiquitin==
-<StructureSection load='3phd' size='340' side='right' caption='[[3phd]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+<StructureSection load='3phd' size='340' side='right'caption='[[3phd]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3phd]] is a 8 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=3PHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PHD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3phd]] is a 8 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=3PHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3c5k|3c5k]], [[3gv4|3gv4]], [[2znv|2znv]], [[3nhe|3nhe]]</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></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC6, KIAA0901, JM21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), UBB, UBA52, UBCEP2, UBC, RPS27A, UBA80, UBCEP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3phd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phd OCA], [https://pdbe.org/3phd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3phd RCSB], [https://www.ebi.ac.uk/pdbsum/3phd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3phd ProSAT]</span></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=3phd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3phd RCSB], [http://www.ebi.ac.uk/pdbsum/3phd PDBsum]</span></td></tr>
 </table>
+== Function ==
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3phd" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Histone deacetylase|Histone deacetylase]]
+*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]]
-*[[Ubiquitin|Ubiquitin]]
+*[[3D structures of ubiquitin|3D structures of ubiquitin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Histone deacetylase]]
 [[Category: Homo sapiens]]
-[[Category: Dong, A]]
+[[Category: Large Structures]]
-[[Category: Kozieradzki, I]]
+[[Category: Dong A]]
-[[Category: Li, F]]
+[[Category: Kozieradzki I]]
-[[Category: Loppnau, P]]
+[[Category: Li F]]
-[[Category: Mackenzie, F]]
+[[Category: Loppnau P]]
-[[Category: Ouyang, H]]
+[[Category: Mackenzie F]]
-[[Category: Qui, W]]
+[[Category: Ouyang H]]
-[[Category: Ravichandran, M]]
+[[Category: Qui W]]
-[[Category: Structural genomic]]
+[[Category: Ravichandran M]]
-[[Category: Schuetz, A]]
+[[Category: Schuetz A]]
-[[Category: Hdac6]]
-[[Category: Protein binding]]
-[[Category: Sgc]]
-[[Category: Ubiquitin]]