5efb: Difference between revisions
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==Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 in complex with oxamflatin== | ==Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 in complex with oxamflatin== | ||
<StructureSection load='5efb' size='340' side='right' caption='[[5efb]], [[Resolution|resolution]] 2.54Å' scene=''> | <StructureSection load='5efb' size='340' side='right'caption='[[5efb]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5efb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFB OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5efb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFB FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.543Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5OK:OXAMFLATIN'>5OK</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5efb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efb OCA], [https://pdbe.org/5efb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efb RCSB], [https://www.ebi.ac.uk/pdbsum/5efb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efb ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/F8W4B7_DANRE F8W4B7_DANRE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5efb" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5efb" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone deacetylase 3D structures|Histone deacetylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Danio rerio]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Christianson DW]] | ||
[[Category: | [[Category: Hai Y]] | ||
Latest revision as of 09:24, 5 July 2023
Crystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 in complex with oxamflatinCrystal structure of Danio rerio histone deacetylase 6 catalytic domain 2 in complex with oxamflatin
Structural highlights
FunctionPublication Abstract from PubMedHistone deacetylase 6 (HDAC6) is a critical target for drug design because of its role in oncogenic transformation and cancer metastasis, and is unique among all histone deacetylases in that it contains tandem catalytic domains designated CD1 and CD2. We now report the crystal structures of CD2 from Homo sapiens HDAC6 and of CD1 and CD2 from Danio rerio HDAC6. We correlated these structures with activity measurements using 13 different substrates. The catalytic activity of CD2 from both species exhibited broad substrate specificity, whereas that of CD1 was highly specific for substrates bearing C-terminal acetyllysine residues. Crystal structures of substrate complexes yielded unprecedented snapshots of the catalytic mechanism. Additionally, crystal structures of complexes with eight different inhibitors, including belinostat and panobinostat (currently used in cancer chemotherapy), the macrocyclic tetrapeptide HC toxin, and the HDAC6-specific inhibitor N-hydroxy-4-(2-((2-hydroxyethyl)(phenyl)amino)-2-oxoethyl)benzamide, revealed surprising new insight regarding changes in Zn2+ coordination and isozyme-specific inhibition. Histone deacetylase 6 structure and molecular basis of catalysis and inhibition.,Hai Y, Christianson DW Nat Chem Biol. 2016 Jul 25. doi: 10.1038/nchembio.2134. PMID:27454933[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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