Abstract
The sequential determination of crystal structures of the SARS coronavirus spike receptor-binding domain (RBD) in complex with its cellular receptor or neutralizing antibody opened a door for the design and development of antiviral competitive inhibitors. Based on those complex structures, we conduct computational characterization and design of RBD-mediated receptor recognition and antibody neutralization. The comparisons between computational predictions and experimental evidences validate our structural bioinformatics protocols. And the calculations predict a number of single substitutions on RBD, receptor or antibody that could remarkably elevate the binding affinities of those complexes. It is reasonable to anticipate our structure-based computation-derived hypotheses could be informative to the future biochemical and immunological tests.
MeSH terms
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Antibodies, Monoclonal / immunology
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Antibodies, Monoclonal / metabolism*
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Antibodies, Viral / immunology
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Antibodies, Viral / metabolism
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Binding Sites, Antibody
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Computational Biology*
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Crystallography, X-Ray
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Drug Design
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Membrane Glycoproteins* / chemistry
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Membrane Glycoproteins* / immunology
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Membrane Glycoproteins* / metabolism
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Neutralization Tests
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Receptors, Virus / immunology
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Receptors, Virus / metabolism*
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Severe acute respiratory syndrome-related coronavirus* / chemistry
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Severe acute respiratory syndrome-related coronavirus* / immunology
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Severe acute respiratory syndrome-related coronavirus* / metabolism
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins* / chemistry
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Viral Envelope Proteins* / immunology
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Viral Envelope Proteins* / metabolism
Substances
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Antibodies, Monoclonal
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Antibodies, Viral
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Membrane Glycoproteins
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Receptors, Virus
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Spike Glycoprotein, Coronavirus
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Viral Envelope Proteins
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spike glycoprotein, SARS-CoV