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Literature summary for 3.2.2.22 extracted from

  • Chan, D.S.; Chu, L.O.; Lee, K.M.; Too, P.H.; Ma, K.W.; Sze, K.H.; Zhu, G.; Shaw, P.C.; Wong, K.B.
    Interaction between trichosanthin, a ribosome-inactivating protein, and the ribosomal stalk protein P2 by chemical shift perturbation and mutagenesis analyses (2007), Nucleic Acids Res., 35, 1660-1672.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
D176A 1.5fold increase in enzyme concentration required for 50% inhibition of protein synthesis Trichosanthes kirilowii
K173A weakened binding to eukaryotic ribosomal protein P2, 7.5fold increase in enzyme concentration required for 50% inhibition of protein synthesis Trichosanthes kirilowii
K173A/R174A/K177A mutant unable to bind to eucaryotic ribosomal protein P2 and to ribosomal stalk in vitro, 18fold less active in inhibition of translation than wild-type Trichosanthes kirilowii
K177A weakened binding to eukaryotic ribosomal protein P2, 3fold increase in enzyme concentration required for 50% inhibition of protein synthesis Trichosanthes kirilowii
R174A weakened binding to eukaryotic ribosomal protein P2, 6fold increase in enzyme concentration required for 50% inhibition of protein synthesis Trichosanthes kirilowii

Organism

Organism UniProt Comment Textmining
Trichosanthes kirilowii P09989
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Subunits

Subunits Comment Organism
More trichosanthin interacts with the C-terminal tail of eukaryotic ribosomal protein P2, involving residues K173, R174, and K177 of trichosanthin Trichosanthes kirilowii