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

Jack Cheng, Tian-Huey Lu*, Chao-Lin Liu and Jung-Yaw Lin

Journal of Biomedical Science 2010, 17:34 doi:10.1186/1423-0127-17-34

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   (2011-06-09 05:42)  National Tsing Hua University email

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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