Comment on "Cleavage mechanism of the H5N1 hemagglutinin by trypsin and furin" [Amino Acids 2008, January 31, Doi: 10.1007/s00726-007-0611-3].
Recently, Guo et al. have reported structural as well as the binding energy data of the particular interactions between the cleavage sites of hemagglutinin and serine proteases, trypsin and furin, using molecular docking approach. Due to a wrong assignment of protonation state on the histidine, one of the catalytic triad in the active site of both enzymes, their docking results are contradictory with the fundamental principle and previous theoretical studies of the known cleavage mechanism in serine proteases.
Rungrotmongkol
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Department of Chemistry, Faculty of Science, Chulalongkorn University, Patumwan, Bangkok, Thailand.
Decha
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P
Malaisree
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Sompornpisut
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P
Hannongbua
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S
D001665:Binding Sites; D045683:Furin / Q000737:chemistry*; D006389:Hemagglutinins, Viral / Q000737:chemistry*; D053124:Influenza A Virus, H5N1 Subtype / Q000737:chemistry* / Q000472:pathogenicity; D008958:Models, Molecular; D008968:Molecular Conformation; D012697:Serine Endopeptidases / Q000737:chemistry; D014357:Trypsin / Q000737:chemistry*
D006389:Hemagglutinins, Viral; D012697:Serine Endopeptidases; D014357:Trypsin; D045683:Furin