Structures and polymorphic interactions of two heptad-repeat regions of the SARS virus S2 protein.
Identifieur interne : 003C88 ( Main/Exploration ); précédent : 003C87; suivant : 003C89Structures and polymorphic interactions of two heptad-repeat regions of the SARS virus S2 protein.
Auteurs : Yiqun Deng [États-Unis] ; Jie Liu ; Qi Zheng ; Wei Yong ; Min LuSource :
- Structure (London, England : 1993) [ 0969-2126 ] ; 2006.
Descripteurs français
- KwdFr :
- Cristallographie aux rayons X, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (génétique), Pliage des protéines, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Structure secondaire des protéines, Structure tertiaire des protéines, Séquences répétées d'acides aminés, Thermodynamique.
- MESH :
- génétique : Glycoprotéines membranaires, Protéines de l'enveloppe virale.
- Cristallographie aux rayons X, Données de séquences moléculaires, Fusion membranaire, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Pliage des protéines, Protéines de l'enveloppe virale, Structure secondaire des protéines, Structure tertiaire des protéines, Séquences répétées d'acides aminés, Thermodynamique.
English descriptors
- KwdEn :
- Crystallography, X-Ray, Membrane Fusion, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid, Spike Glycoprotein, Coronavirus, Thermodynamics, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- Crystallography, X-Ray, Membrane Fusion, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Repetitive Sequences, Amino Acid, Spike Glycoprotein, Coronavirus, Thermodynamics.
Abstract
Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.
DOI: 10.1016/j.str.2006.03.007
PubMed: 16698550
Affiliations:
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J" first="Jie" last="Liu">Jie Liu</name></author><author><name sortKey="Zheng, Qi" sort="Zheng, Qi" uniqKey="Zheng Q" first="Qi" last="Zheng">Qi Zheng</name></author><author><name sortKey="Yong, Wei" sort="Yong, Wei" uniqKey="Yong W" first="Wei" last="Yong">Wei Yong</name></author><author><name sortKey="Lu, Min" sort="Lu, Min" uniqKey="Lu M" first="Min" last="Lu">Min Lu</name></author></analytic><series><title level="j">Structure (London, England : 1993)</title><idno type="ISSN">0969-2126</idno><imprint><date when="2006" type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallography, X-Ray</term><term>Membrane Fusion</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Repetitive Sequences, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Thermodynamics</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Glycoprotéines membranaires (génétique)</term><term>Pliage des protéines</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquences répétées d'acides aminés</term><term>Thermodynamique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glycoprotéines membranaires</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Membrane Fusion</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Repetitive Sequences, Amino Acid</term><term>Spike Glycoprotein, Coronavirus</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Fusion membranaire</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Pliage des protéines</term><term>Protéines de l'enveloppe virale</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquences répétées d'acides aminés</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Entry of SARS coronavirus into its target cell requires large-scale structural transitions in the viral spike (S) glycoprotein in order to induce fusion of the virus and cell membranes. Here we describe the identification and crystal structures of four distinct alpha-helical domains derived from the highly conserved heptad-repeat (HR) regions of the S2 fusion subunit. The four domains are an antiparallel four-stranded coiled coil, a parallel trimeric coiled coil, a four-helix bundle, and a six-helix bundle that is likely the final fusogenic form of the protein. When considered together, the structural and thermodynamic features of the four domains suggest a possible mechanism whereby the HR regions, initially sequestered in the native S glycoprotein spike, are released and refold sequentially to promote membrane fusion. Our results provide a structural framework for understanding the control of membrane fusion and should guide efforts to intervene in the SARS coronavirus entry process.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Liu, Jie" sort="Liu, Jie" uniqKey="Liu J" first="Jie" last="Liu">Jie Liu</name><name sortKey="Lu, Min" sort="Lu, Min" uniqKey="Lu M" first="Min" last="Lu">Min Lu</name><name sortKey="Yong, Wei" sort="Yong, Wei" uniqKey="Yong W" first="Wei" last="Yong">Wei Yong</name><name sortKey="Zheng, Qi" sort="Zheng, Qi" uniqKey="Zheng Q" first="Qi" last="Zheng">Qi Zheng</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Deng, Yiqun" sort="Deng, Yiqun" uniqKey="Deng Y" first="Yiqun" last="Deng">Yiqun Deng</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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