Toggle Main Menu Toggle Search

Open Access padlockePrints

The Newcastle University research output collection, currently available on ePrints, will shortly be moving to a new open repository platform, Figshare. To prepare for the data migration we have paused adding new content to ePrints, and will resume once the new repository is launched. During this time you will continue to have access to ePrints (but no new content will appear). We will share updates here when available.

Structural variability of the ubiquitin specific protease DUSP-UBL double domains

Lookup NU author(s): Dr Martyna PastokORCiD

Downloads

Full text for this publication is not currently held within this repository. Alternative links are provided below where available.

Abstract

USP4, 11 and 15 are three closely related paralogues of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. The DUSP domain and the UBL domain in these proteins are juxtaposed which may provide a functional unit conferring specificity. We determined the structures of the USP15 DUSP-UBL double domain unit in monomeric and dimeric states. We then conducted comparative analysis of the structural and physical properties of all three DUSP-UBL units. We identified structural features that dictate different dispositions between constituent domains, which in turn may influence respective binding properties

Publication metadata

Author(s): Elliott PR, Liu H, Pastok MW, Grossmann GJ, Rigden DJ, Clague MJ, Urbé S, Barsukov IL

Publication type: Article

Publication status: Published

Journal: FEBS Letters

Year: 2011

Volume: 585

Issue: 21

Pages: 3385–3390

Print publication date: 10/10/2011

ISSN (print): 0014-5793

ISSN (electronic): 1873-3468

Publisher: Elsevier BV

URL: http://dx.doi.org/10.1016/j.febslet.2011.09.040

DOI: 10.1016/j.febslet.2011.09.040

Altmetrics

Altmetrics provided by Altmetric

Share