SrasV1, Ncbi, Merge, bibRecord, 001907

Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.

Identifieur interne : 001907 ( Ncbi/Merge ); précédent : 001906; suivant : 001908

Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.

Auteurs : Yuan Zhang [République populaire de Chine] ; Nan Zheng ; Yang Zhong

Source :

Computational biology and chemistry [ 1476-9271 ] ; 2007.

RBID : pubmed:17374510

Descripteurs français

English descriptors

KwdEn :
- Antibodies, Monoclonal (immunology), Antibodies, Monoclonal (metabolism), Antibodies, Viral (immunology), Antibodies, Viral (metabolism), Binding Sites, Antibody, Computational Biology, Crystallography, X-Ray, Drug Design, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Neutralization Tests, Receptors, Virus (immunology), Receptors, Virus (metabolism), SARS Virus (chemistry), SARS Virus (immunology), SARS Virus (metabolism), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology), Viral Envelope Proteins (metabolism).
MESH :
- chemical , chemistry : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Antibodies, Viral, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemical , metabolism : Antibodies, Monoclonal, Antibodies, Viral, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- chemistry : SARS Virus.
- immunology : SARS Virus.
- metabolism : SARS Virus.
- Binding Sites, Antibody, Computational Biology, Crystallography, X-Ray, Drug Design, Neutralization Tests, Spike Glycoprotein, Coronavirus.

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.

DOI: 10.1016/j.compbiolchem.2007.02.005
PubMed: 17374510

Links toward previous steps (curation, corpus...)

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pubmed:17374510

Le document en format XML

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<front><div type="abstract" xml:lang="en">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.</div>
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Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.

Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.

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