2jy8

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[[Image:2jy8.jpg|left|200px]]
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{{Structure
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|GENE= SQSTM1, ORCA, OSIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_2jy8| PDB=2jy8 | SCENE= }}
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|RELATEDENTRY=[[2jy7|2JY7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2jy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jy8 OCA], [http://www.ebi.ac.uk/pdbsum/2jy8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2jy8 RCSB]</span>
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'''NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1) in complex with ubiquitin. RDC refined'''
'''NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1) in complex with ubiquitin. RDC refined'''
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[[Category: Long, J E.]]
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[[Category: ubiquitin associated domain]]
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[[Category: Ubiquitin associated domain]]
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[[Category: ubiquitin binding]]
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Revision as of 06:23, 4 May 2008

Image:2jy8.jpg

Template:STRUCTURE 2jy8

NMR structure of the ubiquitin associated (UBA) domain of p62 (SQSTM1) in complex with ubiquitin. RDC refined


Overview

The p62 protein functions as a scaffold in signaling pathways that lead to activation of NF-kappaB and is an important regulator of osteoclastogenesis. Mutations affecting the receptor activator of NF-kappaB signaling axis can result in human skeletal disorders, including those identified in the C-terminal ubiquitin-associated (UBA) domain of p62 in patients with Paget disease of bone. These observations suggest that the disease may involve a common mechanism related to alterations in the ubiquitin-binding properties of p62. The structural basis for ubiquitin recognition by the UBA domain of p62 has been investigated using NMR and reveals a novel binding mechanism involving a slow exchange structural reorganization of the UBA domain to a "bound" non-canonical UBA conformation that is not significantly populated in the absence of ubiquitin. The repacking of the three-helix bundle generates a binding surface localized around the conserved Xaa-Gly-Phe-Xaa loop that appears to optimize both hydrophobic and electrostatic surface complementarity with ubiquitin. NMR titration analysis shows that the p62-UBA binds to Lys(48)-linked di-ubiquitin with approximately 4-fold lower affinity than to mono-ubiquitin, suggesting preferential binding of the p62-UBA to single ubiquitin units, consistent with the apparent in vivo preference of the p62 protein for Lys(63)-linked polyubiquitin chains (which adopt a more open and extended structure). The conformational switch observed on binding may represent a novel mechanism that underlies specificity in regulating signalinduced protein recognition events.

About this Structure

2JY8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Ubiquitin Recognition by the Ubiquitin-associated Domain of p62 Involves a Novel Conformational Switch., Long J, Gallagher TR, Cavey JR, Sheppard PW, Ralston SH, Layfield R, Searle MS, J Biol Chem. 2008 Feb 29;283(9):5427-5440. Epub 2007 Dec 14. PMID:18083707 Page seeded by OCA on Sun May 4 09:23:40 2008

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