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| | {{STRUCTURE_2jy5| PDB=2jy5 | SCENE= }} | | {{STRUCTURE_2jy5| PDB=2jy5 | SCENE= }} |
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| - | '''NMR structure of Ubiquilin 1 UBA domain'''
| + | ===NMR structure of Ubiquilin 1 UBA domain=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_18241885}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18241885 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18241885}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 2JY5 is a [[Single protein]] structure of 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=2JY5 OCA]. | + | 2JY5 is a [[Single protein]] structure of sequence from [http://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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Uba]] | | [[Category: Uba]] |
| | [[Category: Ubiquilin]] | | [[Category: Ubiquilin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:23:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:24:40 2008'' |
Revision as of 22:24, 28 July 2008
Template:STRUCTURE 2jy5
NMR structure of Ubiquilin 1 UBA domain
Template:ABSTRACT PUBMED 18241885
About this Structure
2JY5 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 29 01:24:40 2008
