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Archived Comments for: A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

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  1. A biophysical elucidation for less toxicity of Agglutinin than Abrin-a from the Seeds of Abrus Precatorius in consequence of crystal structure

    Tian-Huey Lu, National Tsing Hua University

    9 June 2011

    It is a very good article. It is really not easy for my student, Jack, who can finish such a valuable paper in Taiwan.

    We found that Asn200 of abrin-a may form a critical hydrogen bond with G4323 of 28SRNA, while corresponding Pro199 of agglutinin is a kink hydrophobic residue bound with the cleft in a more compact complementary relationship.

    The reason for the lower toxicity of agglutinin than abrin-a might be due to the deformation from inactive to active state of abrin.

    Competing interests

    None declared

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