About: Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin

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About: Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin
Creator	Hilgenfeld, Rolf Lei, Jian
Source	Medline; PMC
abstract	The papain-like protease (PL(pro)) of Middle-East respiratory syndrome coronavirus (MERS-CoV) has proteolytic, deubiquitinating, and deISGylating activities. The latter two are involved in the suppression of the antiviral innate immune response of the host cell. To contribute to an understanding of this process, we present here the X-ray crystal structure of a complex between MERS-CoV PL(pro) and human ubiquitin (Ub) that is devoid of any covalent linkage between the two proteins. Five regions of the PL(pro) bind to two areas of the Ub. The C-terminal five residues of Ub, RLRGG, are similar to the P5–P1 residues of the polyprotein substrates of the PL(pro) and are responsible for the major part of the interaction between the two macromolecules. Through sitedirected mutagenesis, we demonstrate that conserved Asp165 and non-conserved Asp164 are important for the catalytic activities of MERS-CoV PL(pro). The enzyme appears not to be optimized for catalytic efficiency; thus, replacement of Phe269 by Tyr leads to increased peptidolytic and deubiquitinating activities. Ubiquitin binding by MERS-CoV PL(pro) involves remarkable differences compared to the corresponding complex with SARS-CoV PL(pro). The structure and the mutational study help understand common and unique features of the deubiquitinating activity of MERS-CoV PL(pro). ELECTRONIC SUPPLEMENTARY MATERIAL: Supplementary material is available for this article at 10.1007/s12250-016-3742-4 and is accessible for authorized users.
has issue date	2016-05-30(xsd:dateTime)
bibo:doi	10.1007/s12250-016-3742-4
bibo:pmid	27245450
has license	no-cc
sha1sum (hex)	5dd0f03bb34af58c469693cf5f3e311a80d804d4
schema:url	https://doi.org/10.1007/s12250-016-3742-4
resource representing a document's title	Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin
has PubMed Central identifier	PMC7090527
has PubMed identifier	27245450
schema:publication	Virol Sin
resource representing a document's body	covid:5dd0f03bb34af58c469693cf5f3e311a80d804d4#body_text
is schema:about of	named entity 'activities' named entity 'pro' named entity 'mutational' named entity 'pro' named entity 'MERS-CoV' named entity 'PROTEASE' named entity 'SYNDROME' named entity 'HELP' named entity 'PRO' named entity 'PROTEASE' named entity 'CATALYTIC' named entity 'MUTAGENESIS' named entity 'INCREASED' named entity 'CRYSTAL STRUCTURE' named entity 'C-TERMINAL' named entity 'COMPLEX' named entity 'HUMAN' named entity 'REPLACEMENT' named entity 'COMMON' named entity 'DEUBIQUITINATING' named entity 'ACTIVITIES' named entity 'HERE' named entity 'UBIQUITIN' named entity 'AREAS' named entity 'UBIQUITIN BINDING' named entity 'ANTIVIRAL INNATE IMMUNE RESPONSE' named entity 'X-RAY' named entity 'LEADS' named entity 'NON-' named entity 'PAPAIN' named entity 'INTERACTION' named entity 'PROCESS' named entity 'MIDDLE' named entity 'INVOLVED' named entity 'CORONAVIRUS' named entity 'RESPIRATORY' named entity 'LIKE' named entity 'ENZYME' named entity 'RESPIRATORY' named entity 'SIMILAR' named entity 'IMPORTANT' named entity 'PRESENT' named entity 'SUPPRESSION' named entity 'POLYPROTEIN' named entity 'STUDY' named entity 'RESPONSIBLE' named entity 'SARS-COV' named entity 'COMPARED' named entity 'PART OF' named entity 'MACROMOLECULES' named entity 'CATALYTIC EFFICIENCY' named entity 'REGIONS' named entity 'EAST' named entity 'PROTEOLYTIC' named entity 'MUTATIONAL ANALYSIS' named entity 'EAST' named entity 'HUMAN' named entity 'MIDDLE' named entity 'LIKE' named entity 'CORONAVIRUS' named entity 'UBIQUITIN' named entity 'UNDERSTANDING' named entity 'MAJOR PART' named entity 'COVALENT LINKAGE' named entity 'ACTIVITY' named entity 'HOST CELL' named entity 'CONTRIBUTE ' named entity 'STRUCTURE' named entity 'MERS-COV' named entity 'TYR' named entity 'SYNDROME' named entity 'CONSERVED' named entity 'BIND' named entity 'FEATURES' named entity 'PROTEINS' named entity 'UNIQUE' named entity 'INTERACTION' named entity 'PAPAIN' named entity 'STRUCTURAL' covid:arg/5dd0f03bb34af58c469693cf5f3e311a80d804d4

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