SrasV1, Main, Merge, bibRecord, 003E62

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

Identifieur interne : 003E62 ( Main/Merge ); précédent : 003E61; suivant : 003E63

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

Auteurs : Marie-Pierre Egloff [France] ; Hélène Malet ; Akos Putics ; Maarit Heinonen ; Hélène Dutartre ; Antoine Frangeul ; Arnaud Gruez ; Valérie Campanacci ; Christian Cambillau ; John Ziebuhr ; Tero Ahola ; Bruno Canard

Source :

Journal of virology [ 0022-538X ] ; 2006.

RBID : pubmed:16912299

Descripteurs français

English descriptors

KwdEn :
- Adenosine Diphosphate Ribose (analogs & derivatives), Adenosine Diphosphate Ribose (chemistry), Adenosine Diphosphate Ribose (metabolism), Amino Acid Sequence, Crystallography, Hepatitis E virus (chemistry), Hepatitis E virus (metabolism), Histones (chemistry), Histones (metabolism), Models, Molecular, Molecular Sequence Data, Poly Adenosine Diphosphate Ribose (metabolism), Poly(ADP-ribose) Polymerases (metabolism), SARS Virus (chemistry), SARS Virus (metabolism), Semliki forest virus (chemistry), Semliki forest virus (metabolism), Structure-Activity Relationship.
MESH :
- chemical , analogs & derivatives : Adenosine Diphosphate Ribose.
- chemical , chemistry : Adenosine Diphosphate Ribose, Histones.
- chemical , metabolism : Adenosine Diphosphate Ribose, Histones, Poly Adenosine Diphosphate Ribose, Poly(ADP-ribose) Polymerases.
- chemistry : Hepatitis E virus, SARS Virus, Semliki forest virus.
- metabolism : Hepatitis E virus, SARS Virus, Semliki forest virus.
- Amino Acid Sequence, Crystallography, Models, Molecular, Molecular Sequence Data, Structure-Activity Relationship.

Abstract

Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.

Url:

https://hal.archives-ouvertes.fr/hal-02459228

DOI: 10.1128/JVI.00713-06
PubMed: 16912299

Links to Exploration step

pubmed:16912299

Le document en format XML

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<term>Adenosine Diphosphate Ribose (metabolism)</term>
<term>Amino Acid Sequence</term>
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<term>Molecular Sequence Data</term>
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<term>SARS Virus (chemistry)</term>
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<term>Cristallographie</term>
<term>Données de séquences moléculaires</term>
<term>Histone ()</term>
<term>Histone (métabolisme)</term>
<term>Modèles moléculaires</term>
<term>Poly adénosine diphosphate ribose (métabolisme)</term>
<term>Poly(ADP-ribose) polymerases (métabolisme)</term>
<term>Relation structure-activité</term>
<term>Séquence d'acides aminés</term>
<term>Virus de l'hépatite E ()</term>
<term>Virus de l'hépatite E (métabolisme)</term>
<term>Virus de la forêt de Semliki ()</term>
<term>Virus de la forêt de Semliki (métabolisme)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.</div>
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<double doi="10.1128/JVI.00713-06"><HAL><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains</title>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Structural and Functional Basis for ADP-Ribose and Poly(ADP-Ribose) Binding by Viral Macro Domains</title>
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<front><div type="abstract" xml:lang="en">Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.</div>
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EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Merge

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HfdSelect -h $EXPLOR_AREA/Data/Main/Merge/biblio.hfd -nk 003E62 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    Main
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:16912299
   |texte=   Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Merge/RBID.i   -Sk "pubmed:16912299" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Merge/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

Serveur d'exploration SRAS

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains.

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Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki

	Serveur d'exploration SRAS
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.