4a3o: Difference between revisions

No edit summary
No edit summary
 
(5 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:4a3o.jpg|left|200px]]


<!--
==Crystal structure of the USP15 DUSP-UBL monomer==
The line below this paragraph, containing "STRUCTURE_4a3o", creates the "Structure Box" on the page.
<StructureSection load='4a3o' size='340' side='right'caption='[[4a3o]], [[Resolution|resolution]] 2.20&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'>[[4a3o]] is a 2 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=4A3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A3O 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]] 2.2&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
{{STRUCTURE_4a3o|  PDB=4a3o  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a3o OCA], [https://pdbe.org/4a3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a3o RCSB], [https://www.ebi.ac.uk/pdbsum/4a3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a3o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UBP15_HUMAN UBP15_HUMAN] Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling and NF-kappa-B pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes (PubMed:21947082). According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal (PubMed:22344298). Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Protects APC and human papillomavirus type 16 protein E6 against degradation via the ubiquitin proteasome pathway.<ref>PMID:16005295</ref> <ref>PMID:17318178</ref> <ref>PMID:19826004</ref> <ref>PMID:19576224</ref> <ref>PMID:19553310</ref> <ref>PMID:21947082</ref> <ref>PMID:22344298</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties. Structured summary of protein interactions: USP15 and USP15bind by molecular sieving (View Interaction: 1, 2) USP15 and USP15physically interact by molecular sieving (View interaction) USP4 and USP4bind by molecular sieving (View Interaction: 1, 2) USP15 and USP15bind by X ray scattering (View interaction) USP11 and USP11bind by molecular sieving (View interaction) USP4 and USP4bind by nuclear magnetic resonance (View interaction) USP15 and USP15bind by X-ray crystallography (View interaction).


===CRYSTAL STRUCTURE OF THE USP15 DUSP-UBL MONOMER===
Structural variability of the ubiquitin specific protease DUSP-UBL double domains.,Elliott PR, Liu H, Pastok MW, Grossmann GJ, Rigden DJ, Clague MJ, Urbe S, Barsukov IL FEBS Lett. 2011 Nov 4;585(21):3385-90. Epub 2011 Oct 10. PMID:22001210<ref>PMID:22001210</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4a3o" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_22001210}}, adds the Publication Abstract to the page
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 22001210 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_22001210}}
__TOC__
 
</StructureSection>
==About this Structure==
[[4a3o]] 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=4A3O OCA].
 
==Reference==
<ref group="xtra">PMID:022001210</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Ubiquitinyl hydrolase 1]]
[[Category: Large Structures]]
[[Category: Barsukov, I L.]]
[[Category: Barsukov IL]]
[[Category: Clague, M J.]]
[[Category: Clague MJ]]
[[Category: Elliott, P R.]]
[[Category: Elliott PR]]
[[Category: Grossmann, G J.]]
[[Category: Grossmann GJ]]
[[Category: Liu, H.]]
[[Category: Liu H]]
[[Category: Pastok, M W.]]
[[Category: Pastok MW]]
[[Category: Rigden, D J.]]
[[Category: Rigden DJ]]
[[Category: Urbe, S.]]
[[Category: Urbe S]]
[[Category: Hydrolase]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA