5td7
From Proteopedia
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<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=5td7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5td7 OCA], [http://pdbe.org/5td7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5td7 RCSB], [http://www.ebi.ac.uk/pdbsum/5td7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5td7 ProSAT]</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=5td7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5td7 OCA], [http://pdbe.org/5td7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5td7 RCSB], [http://www.ebi.ac.uk/pdbsum/5td7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5td7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cationic polyamines such as spermidine and spermine are critical in all forms of life, as they regulate the function of biological macromolecules. Intracellular polyamine metabolism is regulated by reversible acetylation and dysregulated polyamine metabolism is associated with neoplastic diseases such as colon cancer, prostate cancer and neuroblastoma. Here we report that histone deacetylase 10 (HDAC10) is a robust polyamine deacetylase, using recombinant enzymes from Homo sapiens (human) and Danio rerio (zebrafish). The 2.85 A-resolution crystal structure of zebrafish HDAC10 complexed with a transition-state analogue inhibitor reveals that a glutamate gatekeeper and a sterically constricted active site confer specificity for N8-acetylspermidine hydrolysis and disfavour acetyllysine hydrolysis. Both HDAC10 and spermidine are known to promote cellular survival through autophagy. Accordingly, this work sets a foundation for studying the chemical biology of autophagy through the structure-based design of inhibitors that may also serve as new leads for cancer chemotherapy. | ||
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| + | Histone deacetylase 10 structure and molecular function as a polyamine deacetylase.,Hai Y, Shinsky SA, Porter NJ, Christianson DW Nat Commun. 2017 May 18;8:15368. doi: 10.1038/ncomms15368. PMID:28516954<ref>PMID:28516954</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5td7" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 10:50, 3 August 2017
Crystal structure of histone deacetylase 10
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