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Literature summary for 3.4.21.90 extracted from

  • Tong, L.; Wengler, G.; Rossmann, M.G.
    Refined structure of Sindbis virus core protein and comparison with other chymotrypsin-like serine proteinase structures (1993), J. Mol. Biol., 230, 228-247.
    View publication on PubMed
Search for more literature for 3.4.21.90

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Sindbis virus

Inhibitors

Inhibitors Comment Organism Structure
additional information autoinhibition by the presence of Trp264 side-chain in the S1 pocket after autocatalytic cleavage at Trp264 Sindbis virus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 togavirin has a similar tertiary structure to chymotrypsin Sindbis virus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Sindbis virus core protein + H2O Sindbis virus autocatalytic cleavage at Trp264, . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Sindbis virus
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-
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Sindbis virus core protein + H2O autocatalytic cleavage at Trp264 Sindbis virus Hydrolyzed Sindbis core protein
-
 ?
Sindbis virus core protein + H2O autocatalytic cleavage at Trp264, . Besides its catalytic activity it also plays important roles in the formation of the viral core, the recognition of the spike proteins during the budding process, the recognition and packaging of the viral RNA, and possibly the inhibition of the host cell protein synthesis Sindbis virus ?
-
 ?