What is it about?
Ricin is a highly toxic protein, but an effective small molecular antidote has not been developed yet. We have shown for the first time that a small-molecular inhibitor capable of blocking simultaneously two critical pockets in the toxic protein. We used X-ray crystallography to determine the structural basis for the binding of the inhibitor to the pockets.
Featured Image
Photo by CDC on Unsplash
Why is it important?
This is the first example of a small organic inhibitor that is capable of simultaneously plugging the two critical pockets in the toxic protein. We have revealed that the conformational change in a certain amino acid residue in the toxic protein is an important factor in achieving the interaction between inhibitors and the pockets of the protein.
Perspectives
Read the Original
This page is a summary of: Pterin-based small molecule inhibitor capable of binding to the secondary pocket in the active site of ricin-toxin A chain, PLoS ONE, December 2022, PLOS,
DOI: 10.1371/journal.pone.0277770.
You can read the full text:
Resources
Contributors
The following have contributed to this page