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Prediction of quaternary assembly of SARS coronavirus peplomer.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 2004 Dec 24; Vol. 325 (4), pp. 1210-4. - Publication Year :
- 2004
-
Abstract
- The tertiary structures of the S1 and S2 domains of the spike protein of the coronavirus which is responsible of the severe acute respiratory syndrome (SARS) have been recently predicted. Here a molecular assembly of SARS coronavirus peplomer which accounts for the available functional data is suggested. The interaction between S1 and S2 appears to be stabilised by a large hydrophobic network of aromatic side chains present in both domains. This feature results to be common to all coronaviruses, suggesting potential targeting for drugs preventing coronavirus-related infections.
- Subjects :
- Amino Acid Substitution
Binding Sites
Computer Simulation
Membrane Glycoproteins analysis
Protein Binding
Protein Conformation
Protein Structure, Quaternary
Protein Structure, Tertiary
Spike Glycoprotein, Coronavirus
Structure-Activity Relationship
Viral Envelope Proteins analysis
Membrane Glycoproteins chemistry
Models, Chemical
Models, Molecular
Sequence Analysis, Protein methods
Viral Envelope Proteins chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 325
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 15555555
- Full Text :
- https://doi.org/10.1016/j.bbrc.2004.10.156