Binding and structural studies of the complexes of type 1 ribosome inactivating protein from Momordica balsamina with uracil and uridine

@article{Pandey2019BindingAS,
  title={Binding and structural studies of the complexes of type 1 ribosome inactivating protein from Momordica balsamina with uracil and uridine},
  author={Sada Nand Pandey and Naseer Iqbal and Prashant Kumar Singh and Nilisha Rastogi and Punit Kaur and Sujata Sharma and Tej P. Singh},
  journal={Proteins: Structure},
  year={2019},
  volume={87},
  pages={109 - 99}
}
Ribosome inactivating protein (RIP) catalyzes the cleavage of glycosidic bond formed between adenine and ribose sugar of ribosomal RNA to inactivate ribosomes. Previous structural studies have shown that RNA bases, adenine, guanine, and cytosine tend to bind to RIP in the substrate binding site. However, the mode of binding of uracil with RIP was not yet known. Here, we report crystal structures of two complexes of type 1 RIP from Momordica balsamina (MbRIP1) with base, uracil and nucleoside… 
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This is the first structural evidence of recognition of mRNA cap structures by a ribosome inactivating protein and this action of MbRIP‐1 may have implications for the antiviral activity of this protein in vivo.

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