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Comment
. 2013 May;66(5):464-6.
doi: 10.1016/j.jinf.2012.12.003. Epub 2012 Dec 22.

A predicted receptor-binding and critical neutralizing domain in S protein of the novel human coronavirus HCoV-EMC

Shibo Jiang, Lu Lu, Lanying Du, Asim K Debnath
Comment

A predicted receptor-binding and critical neutralizing domain in S protein of the novel human coronavirus HCoV-EMC

Shibo Jiang et al. J Infect. 2013 May.
No abstract available

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Figures

Figure 1
Figure 1
Prediction of the RBD/CND in the HCoV-EMC S protein S1 subunit based on the RBD in SARS-CoV S protein. (a) Schematic representation of the SARS-CoV S protein. SP, signal peptide; RBD, receptor-binding domain; CND, critical neutralizing domain; FP, fusion peptide; HR, heptad repeat; TM, transmembrane domain; and CP, cytoplasm domain. The residue numbers of each region represent their positions in the S protein of SARS-CoV. (b) Alignment analysis of the sequence of the RBD/CND (residues 321–508) in the SARS-CoV S protein with the corresponding region (residues 377–662) in the HCoV-EMC S protein. The secondary structure assignments are listed above the primary sequence with β-sheets highlighted as arrows and α-helices highlighted by cylinders, respectively. The conserved cysteines are highlighted with red circles. (c) Crystal structures of the RBD/CND in SARS-CoV S protein S1 subunit (1) and predicted structure of RBD/CND in HCoV-EMC S protein S1 subunit (2). A core consists of a five-stranded anti-parallel β-sheet (β1–β4, β7) connecting with three short α-helices (αA–αC), and an extended loop contains two-stranded β-sheet (β5, β6). N* and C* stand for the N- and C-termini of RBD/CND, respectively.
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