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