3gv4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:12, 6 September 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3gv4' size='340' side='right'caption='[[3gv4]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
<StructureSection load='3gv4' size='340' side='right'caption='[[3gv4]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3gv4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GV4 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3gv4]] is a 2 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=3GV4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GV4 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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]] 1.72&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HDAC6, KIAA0901, JM21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone_deacetylase Histone deacetylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3gv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gv4 OCA], [https://pdbe.org/3gv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gv4 RCSB], [https://www.ebi.ac.uk/pdbsum/3gv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gv4 ProSAT]</span></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=3gv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gv4 OCA], [https://pdbe.org/3gv4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gv4 RCSB], [https://www.ebi.ac.uk/pdbsum/3gv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gv4 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
+
[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 28: Line 27:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Histone deacetylase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Arrowsmith, C H]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Bochkarev, A]]
+
[[Category: Bochkarev A]]
-
[[Category: Bountra, C]]
+
[[Category: Bountra C]]
-
[[Category: Dhe-Paganon, S]]
+
[[Category: Dhe-Paganon S]]
-
[[Category: Dong, A]]
+
[[Category: Dong A]]
-
[[Category: Edwards, A M]]
+
[[Category: Edwards AM]]
-
[[Category: Kozieradzki, I]]
+
[[Category: Kozieradzki I]]
-
[[Category: Li, Y]]
+
[[Category: Li Y]]
-
[[Category: Loppnau, P]]
+
[[Category: Loppnau P]]
-
[[Category: MacKenzie, F]]
+
[[Category: MacKenzie F]]
-
[[Category: Min, J]]
+
[[Category: Min J]]
-
[[Category: Ouyang, H]]
+
[[Category: Ouyang H]]
-
[[Category: Ravichandran, M]]
+
[[Category: Ravichandran M]]
-
[[Category: Structural genomic]]
+
[[Category: Weigelt J]]
-
[[Category: Weigelt, J]]
+
-
[[Category: Actin-binding]]
+
-
[[Category: Chromatin regulator]]
+
-
[[Category: Cytoplasm]]
+
-
[[Category: Hdac6]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Nucleus]]
+
-
[[Category: Phosphoprotein]]
+
-
[[Category: Polymorphism]]
+
-
[[Category: Repressor]]
+
-
[[Category: Sgc]]
+
-
[[Category: Transcription]]
+
-
[[Category: Transcription regulation]]
+
-
[[Category: Ubiquitin c-terminal peptide rlrgg]]
+
-
[[Category: Ubl conjugation]]
+
-
[[Category: Zinc]]
+
-
[[Category: Zinc finger]]
+
-
[[Category: Zinc-finger]]
+

Current revision

Crystal structure of human HDAC6 zinc finger domain and ubiquitin C-terminal peptide RLRGG

PDB ID 3gv4

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools