Structural highlights
Publication Abstract from PubMed
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.
Prediction of quaternary assembly of SARS coronavirus peplomer.,Bernini A, Spiga O, Ciutti A, Chiellini S, Bracci L, Yan X, Zheng B, Huang J, He ML, Song HD, Hao P, Zhao G, Niccolai N Biochem Biophys Res Commun. 2004 Dec 24;325(4):1210-4. PMID:15555555[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bernini A, Spiga O, Ciutti A, Chiellini S, Bracci L, Yan X, Zheng B, Huang J, He ML, Song HD, Hao P, Zhao G, Niccolai N. Prediction of quaternary assembly of SARS coronavirus peplomer. Biochem Biophys Res Commun. 2004 Dec 24;325(4):1210-4. PMID:15555555 doi:10.1016/j.bbrc.2004.10.156
