6odb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of HDAC8 in complex with compound 3== | |
| - | + | <StructureSection load='6odb' size='340' side='right'caption='[[6odb]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6odb]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ODB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ODB FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=M8G:N-{2-[(1E)-3-(hydroxyamino)-3-oxoprop-1-en-1-yl]phenyl}-2-phenoxybenzamide'>M8G</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'>[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> | 
| - | [[Category:  | + | <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=6odb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6odb OCA], [http://pdbe.org/6odb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6odb RCSB], [http://www.ebi.ac.uk/pdbsum/6odb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6odb ProSAT]</span></td></tr> | 
| - | [[Category:  | + | </table> | 
| - | [[Category:  | + | == Function == | 
| + | [[http://www.uniprot.org/uniprot/HDAC8_HUMAN HDAC8_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. May play a role in smooth muscle cell contractility.<ref>PMID:10748112</ref> <ref>PMID:10926844</ref> <ref>PMID:10922473</ref> <ref>PMID:14701748</ref>   | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Histone deacetylase]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bair, K]] | ||
| [[Category: Barczak, N]] | [[Category: Barczak, N]] | ||
| - | [[Category:  | + | [[Category: Caravella, J]] | 
| + | [[Category: Conti, C]] | ||
| + | [[Category: Garcia-Dancey, R]] | ||
| [[Category: Han, B]] | [[Category: Han, B]] | ||
| - | [[Category:  | + | [[Category: Hardy, C]] | 
| - | [[Category:  | + | [[Category: Lahdenranta, J]] | 
| + | [[Category: Lancia, D]] | ||
| + | [[Category: Leng, C]] | ||
| + | [[Category: Li, P]] | ||
| + | [[Category: Liu, C]] | ||
| [[Category: Martin, M]] | [[Category: Martin, M]] | ||
| - | [[Category:  | + | [[Category: Ng, P Y]] | 
| - | + | ||
| [[Category: Pardo, E]] | [[Category: Pardo, E]] | ||
| - | [[Category:  | + | [[Category: Rudnitskaya, A]] | 
| - | + | ||
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| - | + | ||
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| [[Category: Saldahna, A]] | [[Category: Saldahna, A]] | ||
| - | [[Category:  | + | [[Category: Tan, T]] | 
| + | [[Category: Thomason, J J]] | ||
| + | [[Category: Toms, A V]] | ||
| + | [[Category: Yao, L]] | ||
| + | [[Category: Zablocki, M M]] | ||
| [[Category: Zhang, C]] | [[Category: Zhang, C]] | ||
| - | [[Category:  | + | [[Category: Zheng, X]] | 
| - | [[Category:  | + | [[Category: Hdac8]] | 
| - | [[Category:  | + | [[Category: Hydrolase]] | 
| - | [[Category:  | + | [[Category: Hydroxamic acid]] | 
Revision as of 09:12, 1 April 2020
Crystal structure of HDAC8 in complex with compound 3
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Categories: Histone deacetylase | Large Structures | Bair, K | Barczak, N | Caravella, J | Conti, C | Garcia-Dancey, R | Han, B | Hardy, C | Lahdenranta, J | Lancia, D | Leng, C | Li, P | Liu, C | Martin, M | Ng, P Y | Pardo, E | Rudnitskaya, A | Saldahna, A | Tan, T | Thomason, J J | Toms, A V | Yao, L | Zablocki, M M | Zhang, C | Zheng, X | Hdac8 | Hydrolase | Hydroxamic acid
