【病毒外文文獻(xiàn)】2013 Crystal structures of Middle East respiratory syndrome coronavirus (MERS-CoV) spike protein

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the distillery SciBX Science Business eXchange Copyright 2013 Nature Publishing Group 1 This week in techniques Approach Summary Licensing status Publication and contact information Drug platforms Crystal structures of Middle East respiratory syndrome coronavirus MERS CoV spike protein Crystal structures of the MERS CoV spike protein in complex with its receptor could aid the development of therapeutics and vaccines against the disease The MERS CoV spike protein engages with dipeptidyl peptidase 4 DPP 4 CD26 expressed on host cells Researchers solved the crystal structures of the MERS CoV spike protein receptor binding domain by itself at 2 5 null resolution and also in complex with DPP 4 at 2 7 null resolution The crystal structures showed that the interaction between the receptor binding domain of the MERS CoV spike protein and DPP 4 is mediated primarily by hydrophilic amino acid residues and that the spike protein receptor binding motif is highly variable Next steps could include using the crystal structures to design compounds that block the spike protein CD26 interaction SciBX 6 30 doi 10 1038 scibx 2013 806 Published online Aug 8 2013 Patent and licensing status unavailable Lu G et al Nature published online July 7 2013 doi 10 1038 nature12328 Contact George F Gao Institute of Microbiology Chinese Academy of Sciences Beijing China e mail gaof