1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
dc.contributor.author | Singh, Chingakham Ranjit | |
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 | 2014-05-01T19:42:58Z | |
dc.date.available | 2014-05-01T19:42:58Z | |
dc.date.issued | 2014-04-01 | |
dc.identifier.citation | Singh, C. R., Lovell, S., Mehzabeen, N., Chowdhury, W. Q., Geanes, E. S., Battaile, K. P. & Roelofs, J. (2014). 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain. Acta Cryst. F70, 418-423. http://dx.doi.org/10.1107/S2053230X14003884 | |
dc.identifier.uri | http://hdl.handle.net/1808/13617 | |
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. | |
dc.description.sponsorship | This work was supported by grants from the Johnson Cancer Research Center, the NIH-NCRR (5P20RR017708 and P20 RR016475) and NIH (8 P20 GM103420 and P20 GM103418). Use of IMCA-CAT was supported by IMCA though a contract with the Hauptman-Woodward MRI. Use of the APS was supported by the US Department of Energy (Contract No. DE-AC02-06CH11357). Publication of this article was funded in part by the Kansas State University Open Access Publishing Fund. | |
dc.publisher | Structural Biology Communications | |
dc.rights | This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. | |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
dc.subject | Nas2 | |
dc.subject | chaperones | |
dc.subject | Proteasome | |
dc.subject | PDZ domain | |
dc.title | 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain | |
dc.type | Article | |
kusw.kuauthor | Lovell, Scott | |
kusw.kuauthor | Mehzabeen, Nurjahan | |
kusw.kudepartment | Protien Structure Lab | |
kusw.oastatus | fullparticipation | |
dc.identifier.doi | 10.1107/S2053230X14003884 | |
kusw.oaversion | Scholarly/refereed, publisher version | |
kusw.oapolicy | This item meets KU Open Access policy criteria. | |
dc.rights.accessrights | openAccess |
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