Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.
Identifieur interne : 000A64 ( PubMed/Corpus ); précédent : 000A63; suivant : 000A65Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.
Auteurs : Jian Lei ; Yuri Kusov ; Rolf HilgenfeldSource :
- Antiviral research [ 1872-9096 ] ; 2018.
English descriptors
- KwdEn :
- Amino Acid Sequence, Coronaviridae (genetics), Coronaviridae (metabolism), Glutamine (chemistry), Humans, Models, Molecular, Papain (chemistry), Papain (metabolism), Protein Binding, Protein Conformation, Protein Domains, Protein Interaction Domains and Motifs, Structure-Activity Relationship, Ubiquitin (chemistry), Ubiquitin (metabolism), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , chemistry : Glutamine, Papain, Ubiquitin, Viral Nonstructural Proteins.
- genetics : Coronaviridae.
- metabolism : Coronaviridae, Papain, Ubiquitin, Viral Nonstructural Proteins.
- Amino Acid Sequence, Humans, Models, Molecular, Protein Binding, Protein Conformation, Protein Domains, Protein Interaction Domains and Motifs, Structure-Activity Relationship.
Abstract
The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called "hypervariable region"), a macrodomain (also named "X domain"), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2pro), the Nsp3 ectodomain (3Ecto, also called "zinc-finger domain"), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.
DOI: 10.1016/j.antiviral.2017.11.001
PubMed: 29128390
Links to Exploration step
pubmed:29128390Le document en format XML
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Electronic address: hilgenfeld@biochem.uni-luebeck.de.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Antiviral research</title><idno type="eISSN">1872-9096</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Coronaviridae (genetics)</term><term>Coronaviridae (metabolism)</term><term>Glutamine (chemistry)</term><term>Humans</term><term>Models, Molecular</term><term>Papain (chemistry)</term><term>Papain (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Domains</term><term>Protein Interaction Domains and Motifs</term><term>Structure-Activity Relationship</term><term>Ubiquitin (chemistry)</term><term>Ubiquitin (metabolism)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutamine</term><term>Papain</term><term>Ubiquitin</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronaviridae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronaviridae</term><term>Papain</term><term>Ubiquitin</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Humans</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Domains</term><term>Protein Interaction Domains and Motifs</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called "hypervariable region"), a macrodomain (also named "X domain"), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2<sup>pro</sup>), the Nsp3 ectodomain (3Ecto, also called "zinc-finger domain"), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29128390</PMID><DateCompleted><Year>2018</Year><Month>06</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN><JournalIssue CitedMedium="Internet"><Volume>149</Volume><PubDate><Year>2018</Year><Month>01</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein.</ArticleTitle><Pagination><MedlinePgn>58-74</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0166-3542(17)30397-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.antiviral.2017.11.001</ELocationID><Abstract><AbstractText>The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called "hypervariable region"), a macrodomain (also named "X domain"), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2<sup>pro</sup>), the Nsp3 ectodomain (3Ecto, also called "zinc-finger domain"), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.</AbstractText><CopyrightInformation>Copyright © 2017 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lei</LastName><ForeName>Jian</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kusov</LastName><ForeName>Yuri</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hilgenfeld</LastName><ForeName>Rolf</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23562 Lübeck, Germany; German Center for Infection Research (DZIF), Hamburg - Lübeck - Borstel - Riems Site, University of Lübeck, Germany. 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