About: Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2

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About: Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2
Creator	Eidhoff, Ulf Gerhartz, Bernd Hassiepen, Ulrich Kroemer, Markus Pierrat, Benoit Renatus, Martin Riedl, Ralph Vinzenz, Daniela Worpenberg, Susanne Arcy, Allan Parrado, Shirley
source	Elsevier; Medline; PMC
abstract	Summary Deubiquitinating proteases reverse protein ubiquitination and rescue their target proteins from destruction by the proteasome. USP2, a cysteine protease and a member of the ubiquitin specific protease family, is overexpressed in prostate cancer and stabilizes fatty acid synthase, which has been associated with the malignancy of some aggressive prostate cancers. Here, we report the structure of the human USP2 catalytic domain in complex with ubiquitin. Ubiquitin uses two major sites for the interaction with the protease. Both sites are required simultaneously, as shown by USP2 inhibition assays with peptides and ubiquitin mutants. In addition, a layer of ordered water molecules mediates key interactions between ubiquitin and USP2. As several of those molecules are found at identical positions in the previously solved USP7/ubiquitin-aldehyde complex structure, we suggest a general mechanism of water-mediated ubiquitin recognition by USPs.
has issue date	2006-08-31(xsd:dateTime)
bibo:doi	10.1016/j.str.2006.06.012
bibo:pmid	16905103
has license	els-covid
sha1sum (hex)	37d0e4a0276b8216314aebc7c21ad4ffc9ddb052
schema:url	https://doi.org/10.1016/j.str.2006.06.012
resource representing a document's title	Structural Basis of Ubiquitin Recognition by the Deubiquitinating Protease USP2
has PubMed Central identifier	PMC7126176
has PubMed identifier	16905103
schema:publication	Structure
resource representing a document's body	covid:37d0e4a0276b8216314aebc7c21ad4ffc9ddb052#body_text
is schema:about of	named entity 'UBIQUITIN' named entity 'cysteine protease' named entity 'protein' named entity 'ubiquitin' named entity 'STRUCTURAL' named entity 'PROTEINS' named entity 'ADDITION' named entity 'STABILIZES' named entity 'IDENTICAL' named entity 'USPS' named entity 'WATER MOLECULES' named entity 'PROTEASES' named entity 'PROTEASE' named entity 'REPORT' named entity 'AGGRESSIVE' named entity 'RECOGNITION' named entity 'USP2' named entity 'HERE' named entity 'USP7' named entity 'COMPLEX' named entity 'PROTEASOME' named entity 'USES' named entity 'MEDIATED' named entity 'MEDIATES' named entity 'UBIQUITIN-ALDEHYDE' named entity 'MEMBER OF' named entity 'DEUBIQUITINATING' named entity 'FAMILY' named entity 'GENERAL' named entity 'PREVIOUSLY' named entity 'CYSTEINE PROTEASE' named entity 'BASIS' named entity 'UBIQUITIN' named entity 'PROTEIN UBIQUITINATION' named entity 'LAYER' named entity 'RESCUE' named entity 'TARGET' named entity 'KEY' named entity 'STRUCTURE' named entity 'MAJOR' named entity 'DESTRUCTION' covid:arg/37d0e4a0276b8216314aebc7c21ad4ffc9ddb052 named entity 'PEPTIDES' named entity 'SPECIFIC' named entity 'INTERACTIONS' named entity 'SIMULTANEOUSLY' named entity 'USP2' named entity 'DEUBIQUITINATING PROTEASE' named entity 'SUGGEST' named entity 'FATTY ACID SYNTHASE' named entity 'THEIR' named entity 'MOLECULES' named entity 'WATER' named entity 'REQUIRED' named entity 'PROSTATE CANCER' named entity 'INHIBITION' named entity 'MECHANISM' named entity 'REVERSE' named entity 'ASSOCIATED WITH' named entity 'HUMAN' named entity 'MUTANTS' named entity 'INTERACTION' named entity 'POSITIONS' named entity 'MALIGNANCY' named entity 'FOUND' named entity 'CATALYTIC DOMAIN' named entity 'SITES' named entity 'RECOGNITION' named entity 'ORDERED' named entity 'ordered' named entity 'synthase'

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