3gv4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3gv4]] is a 2 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=3GV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GV4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3gv4]] is a 2 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=3GV4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GV4 FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
- | <tr><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])</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])</td></tr> |
- | <tr><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='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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gv4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gv4 RCSB], [http://www.ebi.ac.uk/pdbsum/3gv4 PDBsum]</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=3gv4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gv4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gv4 RCSB], [http://www.ebi.ac.uk/pdbsum/3gv4 PDBsum]</span></td></tr> |
- | <table> | + | </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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Histone deacetylase|Histone deacetylase]] | *[[Histone deacetylase|Histone deacetylase]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Histone deacetylase]] | [[Category: Histone deacetylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
- | [[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, A M]] |
- | [[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: | + | [[Category: Structural genomic]] |
- | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Actin-binding]] | [[Category: Actin-binding]] | ||
[[Category: Chromatin regulator]] | [[Category: Chromatin regulator]] | ||
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[[Category: Repressor]] | [[Category: Repressor]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
- | [[Category: Structural genomic]] | ||
- | [[Category: Structural genomics consortium]] | ||
[[Category: Transcription]] | [[Category: Transcription]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] |
Revision as of 09:01, 25 December 2014
Crystal structure of human HDAC6 zinc finger domain and ubiquitin C-terminal peptide RLRGG
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Categories: Histone deacetylase | Homo sapiens | Arrowsmith, C H | Bochkarev, A | Bountra, C | Dhe-Paganon, S | Dong, A | Edwards, A M | Kozieradzki, I | Li, Y | Loppnau, P | MacKenzie, F | Min, J | Ouyang, H | Ravichandran, M | Structural genomic | Weigelt, J | Actin-binding | Chromatin regulator | Hdac6 | Hydrolase | Metal-binding | Nucleus | Phosphoprotein | Repressor | Sgc | Transcription | Transcription regulation | Ubiquitin c-terminal peptide rlrgg | Zinc finger | Zinc-finger