2y5b
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2y5b is ON HOLD Authors: Ye, Y., Akutsu, M., Reyes-Turcu, F., Enchev, R.I., Wilkinson, K.D., Komander, D. Description: Structure of USP21 in comple...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of USP21 in complex with linear diubiquitin-aldehyde== | |
| + | <StructureSection load='2y5b' size='340' side='right'caption='[[2y5b]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2y5b]] 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=2Y5B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y5B 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]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLZ:AMINO-ACETALDEHYDE'>GLZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2y5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y5b OCA], [https://pdbe.org/2y5b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y5b RCSB], [https://www.ebi.ac.uk/pdbsum/2y5b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y5b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/UBP21_HUMAN UBP21_HUMAN] Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates.<ref>PMID:10799498</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Modification of proteins by ubiquitin (Ub) and Ub-like (Ubl) modifiers regulates a variety of cellular functions. The ability of Ub to form chains of eight structurally and functionally distinct types adds further complexity to the system. Ub-specific proteases (USPs) hydrolyse polyUb chains, and some have been suggested to be cross-reactive with Ubl modifiers, such as neural precursor cell expressed, developmentally downregulated 8 (NEDD8) and interferon-stimulated gene 15 (ISG15). Here, we report that USP21 cleaves Ub polymers, and with reduced activity also targets ISG15, but is inactive against NEDD8. A crystal structure of USP21 in complex with linear diUb aldehyde shows how USP21 interacts with polyUb through a previously unidentified second Ub- and ISG15-binding surface on the USP domain core. We also rationalize the inability of USP21 to target NEDD8 and identify differences that allow USPs to distinguish between structurally related modifications. | ||
| - | + | Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21.,Ye Y, Akutsu M, Reyes-Turcu F, Enchev RI, Wilkinson KD, Komander D EMBO Rep. 2011 Apr;12(4):350-7. Epub 2011 Mar 11. PMID:21399617<ref>PMID:21399617</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2y5b" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Thioesterase 3D structures|Thioesterase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Akutsu M]] | ||
| + | [[Category: Enchev RI]] | ||
| + | [[Category: Komander D]] | ||
| + | [[Category: Reyes-Turcu F]] | ||
| + | [[Category: Wilkinson KD]] | ||
| + | [[Category: Ye Y]] | ||
Current revision
Structure of USP21 in complex with linear diubiquitin-aldehyde
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