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Literature summary for 3.4.21.75 extracted from

  • Decha, P.; Rungrotmongkol, T.; Intharathep, P.; Malaisree, M.; Aruksakunwong, O.; Laohpongspaisan, C.; Parasuk, V.; Sompornpisut, P.; Pianwanit, S.; Kokpol, S.; Hannongbua, S.
    Source of high pathogenicity of an Avian influenza virus H5N1: Why H5 is better cleaved by furin (2008), Biophys. J., 95, 128-134.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure of furin with bound decanoyl-Arg-Val-Lys-Arg-chloromethylketone inhibitor Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
decanoyl-Arg-Val-Lys-Arg-chloromethylketone
-
Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hemagglutinin high pathogenic avian influenza virus subtype H5 + H2O hemagglutinin loop of high pathogenic avian influenza virus subtype H5 binds much more tightly into the catalytic site of furin than the hemagglutinin low pathogenic avian influenza virus subtype H3 and hemagglutinin low pathogenic avian influenza virus subtype H5 systems. The -RRRKK- insertion in the hemagglutinin high pathogenic avian influenza virus subtype H5 in particular two arginines at S4 and S6 positions helps directly to hold the hemagglutinin’s cleavage loop in place by forming many strong hydrogen bonds between residues of hemagglutinin and furin Mus musculus ?
-
?
hemagglutinin low pathogenic avian influenza virus subtype H3 + H2O
-
Mus musculus ?
-
?
hemagglutinin low pathogenic avian influenza virus subtype H5 + H2O
-
Mus musculus ?
-
?