title: The structure of ribosome inactivating proteins.
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.
authors.affiliation: Institute of Cellular and Molecular Biology, Department of Chemistry and Biochemistry, 1 University Station A5300, University of Texas, Austin, TX 78712, USA. jrobertus@mail.utexas.edu
authors.forename: Jon D
authors.initials: JD
authors.lastname: Robertus
authors.forename: Arthur F
authors.initials: AF
authors.lastname: Monzingo
mesh_terms: D015195:Drug Design; D006801:Humans; D046911:Macromolecular Substances; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D012270:Ribosomes / Q000187:drug effects*; D012276:Ricin / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism
chemical_list: D046911:Macromolecular Substances; D011506:Proteins; D012276:Ricin