3znh: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[ | ==Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl.== | ||
<StructureSection load='3znh' size='340' side='right' caption='[[3znh]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3znh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cchfi Cchfi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZNH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZNH FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=3znh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3znh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3znh RCSB], [http://www.ebi.ac.uk/pdbsum/3znh PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Active-site directed probes are powerful in studies of enzymatic function. We report an active-site directed probe based on a warhead so far considered unreactive. By replacing the C-terminal carboxylate of ubiquitin (Ub) with an alkyne functionality, a selective reaction with the active-site cysteine residue of de-ubiquitinating enzymes was observed. The resulting product was shown to be a quaternary vinyl thioether, as determined by X-ray crystallography. Proteomic analysis of proteins bound to an immobilized Ub alkyne probe confirmed the selectivity toward de-ubiquitinating enzymes. The observed reactivity is not just restricted to propargylated Ub, as highlighted by the selective reaction between caspase-1 (interleukin converting enzyme) and a propargylated peptide derived from IL-1beta, a caspase-1 substrate. | |||
On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases.,Ekkebus R, van Kasteren SI, Kulathu Y, Scholten A, Berlin I, Geurink PP, de Jong A, Goerdayal S, Neefjes J, Heck AJ, Komander D, Ovaa H J Am Chem Soc. 2013 Feb 15. PMID:23387960<ref>PMID:23387960</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Thioesterase|Thioesterase]] | |||
== | *[[Ubiquitin|Ubiquitin]] | ||
[[ | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cchfi]] | |||
[[Category: Ubiquitinyl hydrolase 1]] | [[Category: Ubiquitinyl hydrolase 1]] | ||
[[Category: Berlin, I | [[Category: Berlin, I]] | ||
[[Category: Ekkebus, R | [[Category: Ekkebus, R]] | ||
[[Category: Goerdayal, G | [[Category: Goerdayal, G]] | ||
[[Category: Heck, A J.R | [[Category: Heck, A J.R]] | ||
[[Category: Komander, D | [[Category: Komander, D]] | ||
[[Category: Kulathu, Y | [[Category: Kulathu, Y]] | ||
[[Category: Neefjes, J | [[Category: Neefjes, J]] | ||
[[Category: Ovaa, H | [[Category: Ovaa, H]] | ||
[[Category: Scholten, A | [[Category: Scholten, A]] | ||
[[Category: DeJong, A | [[Category: DeJong, A]] | ||
[[Category: VanKasteren, S I | [[Category: VanKasteren, S I]] | ||
[[Category: Deubiquitinase]] | [[Category: Deubiquitinase]] | ||
[[Category: Hydrolase-signaling protein complex]] | [[Category: Hydrolase-signaling protein complex]] | ||
Revision as of 18:04, 9 December 2014
Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl.Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl.
Structural highlights
Publication Abstract from PubMedActive-site directed probes are powerful in studies of enzymatic function. We report an active-site directed probe based on a warhead so far considered unreactive. By replacing the C-terminal carboxylate of ubiquitin (Ub) with an alkyne functionality, a selective reaction with the active-site cysteine residue of de-ubiquitinating enzymes was observed. The resulting product was shown to be a quaternary vinyl thioether, as determined by X-ray crystallography. Proteomic analysis of proteins bound to an immobilized Ub alkyne probe confirmed the selectivity toward de-ubiquitinating enzymes. The observed reactivity is not just restricted to propargylated Ub, as highlighted by the selective reaction between caspase-1 (interleukin converting enzyme) and a propargylated peptide derived from IL-1beta, a caspase-1 substrate. On Terminal Alkynes That Can React with Active-Site Cysteine Nucleophiles in Proteases.,Ekkebus R, van Kasteren SI, Kulathu Y, Scholten A, Berlin I, Geurink PP, de Jong A, Goerdayal S, Neefjes J, Heck AJ, Komander D, Ovaa H J Am Chem Soc. 2013 Feb 15. PMID:23387960[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||