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| | ==NMR structure of Ubiquilin 1 UBA domain== | | ==NMR structure of Ubiquilin 1 UBA domain== |
| - | <StructureSection load='2jy5' size='340' side='right'caption='[[2jy5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2jy5' size='340' side='right'caption='[[2jy5]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jy5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JY5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jy5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JY5 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2jy6|2jy6]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UBQLN1, DA41, PLIC1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jy5 OCA], [https://pdbe.org/2jy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jy5 RCSB], [https://www.ebi.ac.uk/pdbsum/2jy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jy5 ProSAT]</span></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=2jy5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jy5 OCA], [https://pdbe.org/2jy5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jy5 RCSB], [https://www.ebi.ac.uk/pdbsum/2jy5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jy5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UBQL1_HUMAN UBQL1_HUMAN]] Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors (By similarity). Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation.
| + | [https://www.uniprot.org/uniprot/UBQL1_HUMAN UBQL1_HUMAN] Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors (By similarity). Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fushman, D]] | + | [[Category: Fushman D]] |
| - | [[Category: Raasi, S]] | + | [[Category: Raasi S]] |
| - | [[Category: Zhang, D]] | + | [[Category: Zhang D]] |
| - | [[Category: Alternative splicing]]
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| - | [[Category: Cytoplasm]]
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| - | [[Category: Nucleus]]
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| - | [[Category: Phosphoprotein]]
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| - | [[Category: Proteasome]]
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| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Uba]]
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| - | [[Category: Ubiquilin]]
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| Structural highlights
Function
UBQL1_HUMAN Links CD47 to the cytoskeleton. Promotes the surface expression of GABA-A receptors (By similarity). Promotes the accumulation of uncleaved PSEN1 and PSEN2 by stimulating their biosynthesis. Has no effect on PSEN1 and PSEN2 degradation.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ubiquilin/PLIC proteins belong to the family of UBL-UBA proteins implicated in the regulation of the ubiquitin-dependent proteasomal degradation of cellular proteins. A human presenilin-interacting protein, ubiquilin-1, has been suggested as potential therapeutic target for treating Huntington's disease. Ubiquilin's interactions with mono- and polyubiquitins are mediated by its UBA domain, which is one of the tightest ubiquitin binders among known ubiquitin-binding domains. Here we report the three-dimensional structure of the UBA domain of ubiquilin-1 (UQ1-UBA) free in solution and in complex with ubiquitin. UQ1-UBA forms a compact three-helix bundle structurally similar to other known UBAs, and binds to the hydrophobic patch on ubiquitin with a K(d) of 20 microM. To gain structural insights into UQ1-UBA's interactions with polyubiquitin chains, we have mapped the binding interface between UQ1-UBA and Lys48- and Lys63-linked di-ubiquitins and characterized the strength of UQ1-UBA binding to these chains. Our NMR data show that UQ1-UBA interacts with the individual ubiquitin units in both chains in a mode similar to its interaction with mono-ubiquitin, although with an improved binding affinity for the chains. Our results indicate that, in contrast to UBA2 of hHR23A that has strong binding preference for Lys48-linked chains, UQ1-UBA shows little or no binding selectivity toward a particular chain linkage or between the two ubiquitin moieties in the same chain. The structural data obtained in this study provide insights into the possible structural reasons for the diversity of polyubiquitin chain recognition by UBA domains.
Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains.,Zhang D, Raasi S, Fushman D J Mol Biol. 2008 Mar 14;377(1):162-80. Epub 2007 Dec 23. PMID:18241885[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang D, Raasi S, Fushman D. Affinity makes the difference: nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J Mol Biol. 2008 Mar 14;377(1):162-80. Epub 2007 Dec 23. PMID:18241885 doi:10.1016/j.jmb.2007.12.029
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