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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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Bibliografiske detaljer
Udgivet i:Biosci Rep
Main Authors: Zhou, Yijun, Li, Xiao-Ping, Kahn, Jennifer N., McLaughlin, John E., Tumer, Nilgun E.
Format: Artigo
Sprog:Inglês
Udgivet: Portland Press Ltd. 2019
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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