SrasV1, PubMed, Curation, bibRecord, 001797

Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.

Identifieur interne : 001797 ( PubMed/Curation ); précédent : 001796; suivant : 001798

Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.

Auteurs : Kailang Wu [États-Unis] ; Weikai Li ; Guiqing Peng ; Fang Li

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2009.

RBID : pubmed:19901337

Descripteurs français

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

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<author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name>
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<term>Humans</term>
<term>Membrane Glycoproteins (chemistry)</term>
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<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>
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Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.

Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.

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