Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein.
Identifieur interne : 000337 ( France/Analysis ); précédent : 000336; suivant : 000338Central 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 BoschSource :
- Virology [ 0042-6822 ] ; 2005.
Descripteurs français
- KwdFr :
- Asparagine (métabolisme), Conformation des protéines, Données de séquences moléculaires, Fusion membranaire (physiologie), Glutamine (métabolisme), Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (métabolisme), Ions (), Ions (métabolisme), Liaison aux protéines, Modèles moléculaires, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (métabolisme), Sels (), Sels (métabolisme), Séquence d'acides aminés, Thermodynamique, Virus du SRAS (), Virus du SRAS (métabolisme), Électricité statique.
- MESH :
- métabolisme : Asparagine, Glutamine, Glycoprotéines membranaires, Ions, Protéines de l'enveloppe virale, Sels, Virus du SRAS.
- physiologie : Fusion membranaire.
- Conformation des protéines, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Ions, Liaison aux protéines, Modèles moléculaires, Protéines de l'enveloppe virale, Sels, Séquence d'acides aminés, Thermodynamique, Virus du SRAS, Électricité statique.
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...)
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- to stream Ncbi, to step Curation: 000F07
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pubmed:15840526Le document en format XML
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Rottier</name></author><author><name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A" last="Rey">Félix A. Rey</name></author><author><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Asparagine (metabolism)</term><term>Glutamine (metabolism)</term><term>Ions (chemistry)</term><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><term>SARS Virus (chemistry)</term><term>SARS Virus (metabolism)</term><term>Salts (chemistry)</term><term>Salts (metabolism)</term><term>Spike Glycoprotein, Coronavirus</term><term>Static Electricity</term><term>Thermodynamics</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Asparagine (métabolisme)</term><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></keywords><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></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Asparagine</term><term>Glutamine</term><term>Ions</term><term>Membrane Glycoproteins</term><term>Salts</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Asparagine</term><term>Glutamine</term><term>Glycoprotéines membranaires</term><term>Ions</term><term>Protéines de l'enveloppe virale</term><term>Sels</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Fusion membranaire</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Membrane Fusion</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Conformation</term><term>Spike Glycoprotein, Coronavirus</term><term>Static Electricity</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Ions</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Protéines de l'enveloppe virale</term><term>Sels</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Virus du SRAS</term><term>Électricité statique</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><affiliations><list><country><li>France</li></country><region><li>Île-de-France</li></region><settlement><li>Gif-sur-Yvette</li></settlement></list><tree><noCountry><name sortKey="Bosch, Berend Jan" sort="Bosch, Berend Jan" uniqKey="Bosch B" first="Berend Jan" last="Bosch">Berend Jan Bosch</name><name sortKey="Rey, Felix A" sort="Rey, Felix A" uniqKey="Rey F" first="Félix A" last="Rey">Félix A. Rey</name><name sortKey="Rottier, Peter J M" sort="Rottier, Peter J M" uniqKey="Rottier P" first="Peter J M" last="Rottier">Peter J M. Rottier</name><name sortKey="Vigouroux, Armelle" sort="Vigouroux, Armelle" uniqKey="Vigouroux A" first="Armelle" last="Vigouroux">Armelle Vigouroux</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Duquerroy, Stephane" sort="Duquerroy, Stephane" uniqKey="Duquerroy S" first="Stéphane" last="Duquerroy">Stéphane Duquerroy</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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