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Leucine 232 and hydrophobic residues at the ribosomal P stalk binding site are critical for biological activity of ricin
Ricin interacts with the ribosomal P stalk to cleave a conserved adenine from the α-sarcin/ricin loop (SRL) of the rRNA. Ricin toxin A chain (RTA) uses Arg(235) as the most critical arginine for binding to the P stalk through electrostatic interactions to facilitate depurination. Structural analysis...
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| Udgivet i: | Biosci Rep |
|---|---|
| Main Authors: | , , , , |
| Format: | Artigo |
| Sprog: | Inglês |
| Udgivet: |
Portland Press Ltd.
2019
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| Fag: | |
| Online adgang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6822507/ https://ncbi.nlm.nih.gov/pubmed/31548364 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BSR20192022 |
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