title: [Ribosomal antibiotics].
abstract: In spite of decades of research, our understanding of the principles of antibiotic binding to the ribosome and the mechanisms of drug action remains only fragmentary. Recent progress in biochemical and genetic studies of some "old" and new antibiotics and the availability of high-resolution structures of the ribosome subunits allows mapping the antibiotic-binding sites at atomic resolution. In this review, interaction of three groups of antibiotics with the ribosome and the mechanisms of the drug action are discussed, considering the data used to map the binding sites of the new macrolide derivatives, ketolides, a novel clinically important antibiotic linezolid, and a still experimental drug evernimicin.
authors.affiliation: Center for Pharmaceutical Biotechnology-m/c 870, University of Illinois, Chicago, Illinois 60607, USA. shura@uic.edu
authors.forename: A S
authors.initials: AS
authors.lastname: Man'kin
mesh_terms: D000081:Acetamides / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology*; D001665:Binding Sites / Q000235:genetics; D004351:Drug Resistance; D006801:Humans; D048628:Ketolides; D000069349:Linezolid; D018942:Macrolides; D009154:Mutation; D023303:Oxazolidinones / Q000378:metabolism / Q000494:pharmacology; D014176:Protein Biosynthesis / Q000187:drug effects; D011500:Protein Synthesis Inhibitors / Q000378:metabolism / Q000494:pharmacology; D012270:Ribosomes / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism
chemical_list: D000081:Acetamides; D000900:Anti-Bacterial Agents; D048628:Ketolides; D018942:Macrolides; D023303:Oxazolidinones; D011500:Protein Synthesis Inhibitors; D000069349:Linezolid; C106791:telithromycin
vernacular_title: Ribosomnye antibiotiki.