Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.
Identifieur interne : 002B48 ( Main/Exploration ); précédent : 002B47; suivant : 002B49Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.
Auteurs : Kailang Wu [États-Unis] ; Weikai Li ; Guiqing Peng ; Fang LiSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.
Descripteurs français
- KwdFr :
- Coronavirus (), Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Humains, Liaison aux protéines, Modèles moléculaires, Peptidyl-Dipeptidase A (), Protéines de l'enveloppe virale (), Sites de fixation, Structure quaternaire des protéines, Structure secondaire des protéines, Séquence d'acides aminés.
- MESH :
- Coronavirus, Cristallographie aux rayons X, Données de séquences moléculaires, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Humains, Liaison aux protéines, Modèles moléculaires, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Sites de fixation, Structure quaternaire des protéines, Structure secondaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites, Coronavirus (chemistry), Crystallography, X-Ray, Humans, Membrane Glycoproteins (chemistry), Models, Molecular, Molecular Sequence Data, Peptidyl-Dipeptidase A (chemistry), Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Membrane Glycoproteins, Peptidyl-Dipeptidase A, Viral Envelope Proteins.
- chemistry : Coronavirus.
- Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Quaternary, Protein Structure, Secondary, Spike Glycoprotein, Coronavirus.
Abstract
NL63 coronavirus (NL63-CoV), a prevalent human respiratory virus, is the only group I coronavirus known to use angiotensin-converting enzyme 2 (ACE2) as its receptor. Incidentally, ACE2 is also used by group II SARS coronavirus (SARS-CoV). We investigated how different groups of coronaviruses recognize the same receptor, whereas homologous group I coronaviruses recognize different receptors. We determined the crystal structure of NL63-CoV spike protein receptor-binding domain (RBD) complexed with human ACE2. NL63-CoV RBD has a novel beta-sandwich core structure consisting of 2 layers of beta-sheets, presenting 3 discontinuous receptor-binding motifs (RBMs) to bind ACE2. NL63-CoV and SARS-CoV have no structural homology in RBD cores or RBMs; yet the 2 viruses recognize common ACE2 regions, largely because of a "virus-binding hotspot" on ACE2. Among group I coronaviruses, RBD cores are conserved but RBMs are variable, explaining how these viruses recognize different receptors. These results provide a structural basis for understanding viral evolution and virus-receptor interactions.
DOI: 10.1073/pnas.0908837106
PubMed: 19901337
Affiliations:
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type="wicri:Area/Main/Exploration">002B48</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.</title><author><name sortKey="Wu, Kailang" sort="Wu, Kailang" uniqKey="Wu K" first="Kailang" last="Wu">Kailang Wu</name><affiliation wicri:level="2"><nlm:affiliation>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455</wicri:regionArea><placeName><region type="state">Minnesota</region></placeName></affiliation></author><author><name sortKey="Li, Weikai" sort="Li, Weikai" uniqKey="Li W" first="Weikai" last="Li">Weikai Li</name></author><author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Coronavirus (chemistry)</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Membrane Glycoproteins (chemistry)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Peptidyl-Dipeptidase A (chemistry)</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Coronavirus ()</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires ()</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A ()</term><term>Protéines de l'enveloppe virale ()</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptidyl-Dipeptidase A</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites</term><term>Crystallography, X-Ray</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Quaternary</term><term>Protein Structure, Secondary</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Coronavirus</term><term>Cristallographie aux rayons X</term><term>Données de séquences moléculaires</term><term>Glycoprotéine de spicule des coronavirus</term><term>Glycoprotéines membranaires</term><term>Humains</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Sites de fixation</term><term>Structure quaternaire des protéines</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">NL63 coronavirus (NL63-CoV), a prevalent human respiratory virus, is the only group I coronavirus known to use angiotensin-converting enzyme 2 (ACE2) as its receptor. Incidentally, ACE2 is also used by group II SARS coronavirus (SARS-CoV). We investigated how different groups of coronaviruses recognize the same receptor, whereas homologous group I coronaviruses recognize different receptors. We determined the crystal structure of NL63-CoV spike protein receptor-binding domain (RBD) complexed with human ACE2. NL63-CoV RBD has a novel beta-sandwich core structure consisting of 2 layers of beta-sheets, presenting 3 discontinuous receptor-binding motifs (RBMs) to bind ACE2. NL63-CoV and SARS-CoV have no structural homology in RBD cores or RBMs; yet the 2 viruses recognize common ACE2 regions, largely because of a "virus-binding hotspot" on ACE2. Among group I coronaviruses, RBD cores are conserved but RBMs are variable, explaining how these viruses recognize different receptors. These results provide a structural basis for understanding viral evolution and virus-receptor interactions.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Minnesota</li></region></list><tree><noCountry><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><name sortKey="Li, Weikai" sort="Li, Weikai" uniqKey="Li W" first="Weikai" last="Li">Weikai Li</name><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name></noCountry><country name="États-Unis"><region name="Minnesota"><name sortKey="Wu, Kailang" sort="Wu, Kailang" uniqKey="Wu K" first="Kailang" last="Wu">Kailang Wu</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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