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[[Image:1xd3.png|left|200px]]


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==Crystal structure of UCHL3-UbVME complex==
The line below this paragraph, containing "STRUCTURE_1xd3", creates the "Structure Box" on the page.
<StructureSection load='1xd3' size='340' side='right'caption='[[1xd3]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1xd3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XD3 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GVE:METHYL+4-AMINOBUTANOATE'>GVE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1xd3|  PDB=1xd3  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xd3 OCA], [https://pdbe.org/1xd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xd3 RCSB], [https://www.ebi.ac.uk/pdbsum/1xd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xd3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UCHL3_HUMAN UCHL3_HUMAN] Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3", and exhibits a preference towards 'Lys-48'-linked Ubiquitin chains. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-signaling and insulin-induced adipogenesis. Required for stress-response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders.<ref>PMID:2530630</ref> <ref>PMID:9790970</ref> <ref>PMID:19154770</ref> <ref>PMID:21762696</ref> <ref>PMID:22689415</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xd/1xd3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xd3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ubiquitin C-terminal hydrolases (UCHs) comprise a family of small ubiquitin-specific proteases of uncertain function. Although no cellular substrates have been identified for UCHs, their highly tissue-specific expression patterns and the association of UCH-L1 mutations with human disease strongly suggest a critical role. The structure of the yeast UCH Yuh1-ubiquitin aldehyde complex identified an active site crossover loop predicted to limit the size of suitable substrates. We report the 1.45 A resolution crystal structure of human UCH-L3 in complex with the inhibitor ubiquitin vinylmethylester, an inhibitor that forms a covalent adduct with the active site cysteine of ubiquitin-specific proteases. This structure confirms the predicted mechanism of the inhibitor and allows the direct comparison of a UCH family enzyme in the free and ligand-bound state. We also show the efficient hydrolysis by human UCH-L3 of a 13-residue peptide in isopeptide linkage with ubiquitin, consistent with considerable flexibility in UCH substrate size. We propose a model for the catalytic cycle of UCH family members which accounts for the hydrolysis of larger ubiquitin conjugates.


===Crystal structure of UCHL3-UbVME complex===
Structure of the ubiquitin hydrolase UCH-L3 complexed with a suicide substrate.,Misaghi S, Galardy PJ, Meester WJ, Ovaa H, Ploegh HL, Gaudet R J Biol Chem. 2005 Jan 14;280(2):1512-20. Epub 2004 Nov 5. PMID:15531586<ref>PMID:15531586</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1xd3" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15531586}}, adds the Publication Abstract to the page
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15531586 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15531586}}
__TOC__
 
</StructureSection>
==About this Structure==
[[1xd3]] is a 4 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=1XD3 OCA].
 
==Reference==
<ref group="xtra">PMID:15531586</ref><ref group="xtra">PMID:12401499</ref><ref group="xtra">PMID:11566882</ref><ref group="xtra">PMID:9233788</ref><ref group="xtra">PMID:10406793</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Large Structures]]
[[Category: Galardy, P J.]]
[[Category: Galardy PJ]]
[[Category: Gaudet, R.]]
[[Category: Gaudet R]]
[[Category: Meester, W J.N.]]
[[Category: Meester WJN]]
[[Category: Misaghi, S.]]
[[Category: Misaghi S]]
[[Category: Ovaa, H.]]
[[Category: Ovaa H]]
[[Category: Ploegh, H L.]]
[[Category: Ploegh HL]]
[[Category: Active site crossover loop]]
[[Category: Enzyme-ligand complex]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/1xd3"