Abstract
Ribosome Inactivating Proteins, RIPs, depurinate an invariant adenine from the 28S rRNA of eukaryotic ribosomes; they have evolved to near enzymatic perfection for this task. The N-glycosidase fold is conserved in plant and bacterial enzymes. RIPs can form complexes with cell surface recognition proteins that dramatically increase the cytotoxicity of the molecule.
Keywords: ribosome inactivating proteins, 28s rrna, eukaryotic ribosomes
Mini-Reviews in Medicinal Chemistry
Title: The Structure of Ribosome Inactivating Proteins
Volume: 4 Issue: 5
Author(s): Jon D. Robertus and Arthur F. Monzingo
Affiliation:
Keywords: ribosome inactivating proteins, 28s rrna, eukaryotic ribosomes
Abstract: Ribosome Inactivating Proteins, RIPs, depurinate an invariant adenine from the 28S rRNA of eukaryotic ribosomes; they have evolved to near enzymatic perfection for this task. The N-glycosidase fold is conserved in plant and bacterial enzymes. RIPs can form complexes with cell surface recognition proteins that dramatically increase the cytotoxicity of the molecule.
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Cite this article as:
Robertus D. Jon and Monzingo F. Arthur, The Structure of Ribosome Inactivating Proteins, Mini-Reviews in Medicinal Chemistry 2004; 4 (5) . https://dx.doi.org/10.2174/1389557043403837
DOI https://dx.doi.org/10.2174/1389557043403837 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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