4fvt: Difference between revisions
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[[ | ==Human SIRT3 bound to Ac-ACS peptide and Carba-NAD== | ||
<StructureSection load='4fvt' size='340' side='right' caption='[[4fvt]], [[Resolution|resolution]] 2.47Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fvt]] 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=4FVT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FVT FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CNA:CARBA-NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>CNA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4g1c|4g1c]]</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=4fvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fvt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fvt RCSB], [http://www.ebi.ac.uk/pdbsum/4fvt PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Carba-NAD is a synthetic compound identical to NAD except for one substitution, where an oxygen atom adjacent to the anomeric linkage bearing nicotinamide is replaced with a methylene group. Because it is inert in nicotinamide displacement reactions, carba-NAD is an unreactive substrate analogue for NAD consuming enzymes. SIRT3 and SIRT5 are NAD consuming enzymes that are potential therapeutic targets for the treatment of metabolic diseases and cancers. We report an improved carba-NAD synthesis, including a pyrophosphate coupling method that proceeds in approximately 60% yield. We also disclose the x-ray crystal structures of the ternary complexes of SIRT3 and SIRT5 bound to a peptide substrate and carba-NAD. These x-ray crystal structures provide critical snapshots of the mechanism by which human sirtuins function as protein deacylation catalysts. | |||
Synthesis of Carba-NAD and the Structures of Its Ternary Complexes with SIRT3 and SIRT5.,Szczepankiewicz BG, Dai H, Koppetsch KJ, Qian D, Jiang F, Mao C, Perni RB J Org Chem. 2012 Jul 31. PMID:22849721<ref>PMID:22849721</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Dai, H.]] | [[Category: Dai, H.]] | ||
Revision as of 09:51, 25 June 2014
Human SIRT3 bound to Ac-ACS peptide and Carba-NADHuman SIRT3 bound to Ac-ACS peptide and Carba-NAD
Structural highlights
Publication Abstract from PubMedCarba-NAD is a synthetic compound identical to NAD except for one substitution, where an oxygen atom adjacent to the anomeric linkage bearing nicotinamide is replaced with a methylene group. Because it is inert in nicotinamide displacement reactions, carba-NAD is an unreactive substrate analogue for NAD consuming enzymes. SIRT3 and SIRT5 are NAD consuming enzymes that are potential therapeutic targets for the treatment of metabolic diseases and cancers. We report an improved carba-NAD synthesis, including a pyrophosphate coupling method that proceeds in approximately 60% yield. We also disclose the x-ray crystal structures of the ternary complexes of SIRT3 and SIRT5 bound to a peptide substrate and carba-NAD. These x-ray crystal structures provide critical snapshots of the mechanism by which human sirtuins function as protein deacylation catalysts. Synthesis of Carba-NAD and the Structures of Its Ternary Complexes with SIRT3 and SIRT5.,Szczepankiewicz BG, Dai H, Koppetsch KJ, Qian D, Jiang F, Mao C, Perni RB J Org Chem. 2012 Jul 31. PMID:22849721[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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