Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.
Identifieur interne : 001907 ( Ncbi/Merge ); précédent : 001906; suivant : 001908Computational characterization and design of SARS coronavirus receptor recognition and antibody neutralization.
Auteurs : Yuan Zhang [République populaire de Chine] ; Nan Zheng ; Yang ZhongSource :
- Computational biology and chemistry [ 1476-9271 ] ; 2007.
Descripteurs français
- KwdFr :
- Anticorps antiviraux (immunologie), Anticorps antiviraux (métabolisme), Anticorps monoclonaux (immunologie), Anticorps monoclonaux (métabolisme), Biologie informatique, Conception de médicament, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires (), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (immunologie), Protéines de l'enveloppe virale (métabolisme), Récepteurs viraux (immunologie), Récepteurs viraux (métabolisme), Sites de fixation des anticorps, Tests de neutralisation, Virus du SRAS (), Virus du SRAS (immunologie), Virus du SRAS (métabolisme).
- MESH :
- immunologie : Anticorps antiviraux, Anticorps monoclonaux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- métabolisme : Anticorps antiviraux, Anticorps monoclonaux, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Récepteurs viraux, Virus du SRAS.
- Biologie informatique, Conception de médicament, Cristallographie aux rayons X, Glycoprotéine de spicule des coronavirus, Glycoprotéines membranaires, Protéines de l'enveloppe virale, Sites de fixation des anticorps, Tests de neutralisation, Virus du SRAS.
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
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pubmed:17374510Le 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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