SrasV1, PubMed, Checkpoint, bibRecord, 002804

Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.

Identifieur interne : 002804 ( PubMed/Checkpoint ); précédent : 002803; suivant : 002805

Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.

Auteurs : Stéphane Duquerroy [France] ; Armelle Vigouroux ; Peter J M. Rottier ; Félix A. Rey ; Berend Jan Bosch

Source :

Virology [ 0042-6822 ] ; 2005.

RBID : pubmed:15840526

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Asparagine (metabolism), Glutamine (metabolism), Ions (chemistry), Ions (metabolism), Membrane Fusion (physiology), Membrane Glycoproteins (chemistry), Membrane Glycoproteins (metabolism), Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, SARS Virus (chemistry), SARS Virus (metabolism), Salts (chemistry), Salts (metabolism), Spike Glycoprotein, Coronavirus, Static Electricity, Thermodynamics, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (metabolism).
MESH :
- chemical , chemistry : Ions, Membrane Glycoproteins, Salts, Viral Envelope Proteins.
- chemical , metabolism : Asparagine, Glutamine, Ions, Membrane Glycoproteins, Salts, Viral Envelope Proteins.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- physiology : Membrane Fusion.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation, Spike Glycoprotein, Coronavirus, Static Electricity, Thermodynamics.

Abstract

The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.

DOI: 10.1016/j.virol.2005.02.022
PubMed: 15840526

Affiliations:

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 002779
to stream PubMed, to step Curation: 002779

Links to Exploration step

pubmed:15840526

Le document en format XML

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<term>Ions (metabolism)</term>
<term>Membrane Fusion (physiology)</term>
<term>Membrane Glycoproteins (chemistry)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
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<term>SARS Virus (metabolism)</term>
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<term>Salts (metabolism)</term>
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<term>Thermodynamics</term>
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<term>Conformation des protéines</term>
<term>Données de séquences moléculaires</term>
<term>Fusion membranaire (physiologie)</term>
<term>Glutamine (métabolisme)</term>
<term>Glycoprotéine de spicule des coronavirus</term>
<term>Glycoprotéines membranaires ()</term>
<term>Glycoprotéines membranaires (métabolisme)</term>
<term>Ions ()</term>
<term>Ions (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines de l'enveloppe virale ()</term>
<term>Protéines de l'enveloppe virale (métabolisme)</term>
<term>Sels ()</term>
<term>Sels (métabolisme)</term>
<term>Séquence d'acides aminés</term>
<term>Thermodynamique</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (métabolisme)</term>
<term>Électricité statique</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ions</term>
<term>Membrane Glycoproteins</term>
<term>Salts</term>
<term>Viral Envelope Proteins</term>
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<term>Salts</term>
<term>Viral Envelope Proteins</term>
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<term>Protéines de l'enveloppe virale</term>
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<front><div type="abstract" xml:lang="en">The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.</div>
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<Abstract><AbstractText>The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.</AbstractText>
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<ReferenceList><Reference><Citation>J Virol. 2003 Aug;77(16):8801-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12885899</ArticleId>
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</ReferenceList>
<ReferenceList><Reference><Citation>J Struct Biol. 2002 Jan-Feb;137(1-2):54-64</Citation>
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</Reference>
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<ReferenceList><Reference><Citation>Biochemistry. 2004 Nov 9;43(44):14064-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15518555</ArticleId>
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   |texte=   Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.
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Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.

Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.

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