View source for 4bou


==Structure of OTUD3 OTU domain==
<StructureSection load='4bou' size='340' side='right'caption='[[4bou]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bou]] is a 1 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=4BOU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BOU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55&#8491;</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=4bou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bou OCA], [https://pdbe.org/4bou PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bou RCSB], [https://www.ebi.ac.uk/pdbsum/4bou PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bou ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OTUD3_HUMAN OTUD3_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sixteen ovarian tumor (OTU) family deubiquitinases (DUBs) exist in humans, and most members regulate cell-signaling cascades. Several OTU DUBs were reported to be ubiquitin (Ub) chain linkage specific, but comprehensive analyses are missing, and the underlying mechanisms of linkage specificity are unclear. Using Ub chains of all eight linkage types, we reveal that most human OTU enzymes are linkage specific, preferring one, two, or a defined subset of linkage types, including unstudied atypical Ub chains. Biochemical analysis and five crystal structures of OTU DUBs with or without Ub substrates reveal four mechanisms of linkage specificity. Additional Ub-binding domains, the ubiquitinated sequence in the substrate, and defined S1' and S2 Ub-binding sites on the OTU domain enable OTU DUBs to distinguish linkage types. We introduce Ub chain restriction analysis, in which OTU DUBs are used as restriction enzymes to reveal linkage type and the relative abundance of Ub chains on substrates.

OTU Deubiquitinases Reveal Mechanisms of Linkage Specificity and Enable Ubiquitin Chain Restriction Analysis.,Mevissen TE, Hospenthal MK, Geurink PP, Elliott PR, Akutsu M, Arnaudo N, Ekkebus R, Kulathu Y, Wauer T, El Oualid F, Freund SM, Ovaa H, Komander D Cell. 2013 Jul 3;154(1):169-84. doi: 10.1016/j.cell.2013.05.046. PMID:23827681<ref>PMID:23827681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bou" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Akutsu M]]
[[Category: Arnaudo N]]
[[Category: Ekkebus R]]
[[Category: El Oualid F]]
[[Category: Elliott PR]]
[[Category: Freund SMV]]
[[Category: Geurink PP]]
[[Category: Hospenthal MK]]
[[Category: Komander D]]
[[Category: Kulathu Y]]
[[Category: Mevissen TET]]
[[Category: Ovaa H]]
[[Category: Wauer T]]