1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain

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dc.contributor.author Singh, Chingakham R.
dc.contributor.author Lovell, Scott
dc.contributor.author Mehzabeen, Nurjahan
dc.contributor.author Chowdhury, Wasimul Q.
dc.contributor.author Geanes, Eric S.
dc.contributor.author Battaile, Kevin P.
dc.contributor.author Roelofs, Jeroen
dc.date.accessioned 2014-05-28T21:33:56Z
dc.date.available 2014-05-28T21:33:56Z
dc.date.issued 2014-05-28
dc.identifier.uri http://hdl.handle.net/2097/17799
dc.description.abstract The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-terminus of Rpt5 for binding. Here, the 1.15 Å resolution structure of the PDZ domain of Nas2 is reported. This structure will provide a basis for further insights regarding the structure and function of Nas2 in proteasome assembly. en_US
dc.language.iso en_US en_US
dc.relation.uri http://scripts.iucr.org/cgi-bin/paper?S2053230X14003884 en_US
dc.rights This open-access article is distributed under the terms of the Creative Commons Attribution Licence http://creativecommons.org/licenses/by/2.0/uk/legalcode, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. en_US
dc.subject 26S proteasome en_US
dc.subject Proteasome-assembly en_US
dc.subject Nas2 PDZ domain en_US
dc.title 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain en_US
dc.type Article (publisher version) en_US
dc.date.published 2014 en_US
dc.citation.doi doi:10.1107/S2053230X14003884 en_US
dc.citation.epage 423 en_US
dc.citation.issue 4 en_US
dc.citation.jtitle Acta Crystallographica.Section F, Structural Biology Communications en_US
dc.citation.spage 418 en_US
dc.citation.volume 70 en_US
dc.contributor.authoreid csingh en_US
dc.contributor.authoreid jroelofs en_US

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