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Comparative Study
. 2004 Dec 24;325(4):1210-4.
doi: 10.1016/j.bbrc.2004.10.156.

Prediction of quaternary assembly of SARS coronavirus peplomer

Andrea Bernini  1 , Ottavia Spiga, Arianna Ciutti, Stefano Chiellini, Luisa Bracci, Xiyun Yan, Bojian Zheng, Jiandong Huang, Ming-Liang He, Huai-Dong Song, Pei Hao, Guoping Zhao, Neri Niccolai
Affiliations
Comparative Study

Prediction of quaternary assembly of SARS coronavirus peplomer

Andrea Bernini et al. Biochem Biophys Res Commun. .

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.

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Figures

Fig. 1
Fig. 1
The S1 domain oriented to fit the morphological SEM images of . In yellow and in red the potential N-glycosylation sites and the residues involved in the interaction with ACE2 are, respectively, colored. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this paper.)
Fig. 2
Fig. 2
A detailed representation of the S1 (dark blue) hydrophobic pocket interacting with the S2 (pale blue) finger. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this paper.)
Fig. 3
Fig. 3
Three spike glycoproteins form the peplomer of SARS-CoV coronavirus.
See this image and copyright information in PMC

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