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ID: 265064.0, MPI für molekulare Genetik / Ribosome Research Groups
Species-specific antibiotic-ribosome interactions: implications for drug development
Authors:Wilson, Daniel N.; Harms, Jörg M.; Nierhaus, Knud H.; Schlünzen, Frank; Fucini, Paola
Language:English
Date of Publication (YYYY-MM-DD):2005-12
Title of Journal:Biological Chemistry Hoppe-Seyler (Berlin)
Journal Abbrev.:Biol Chem Hoppe Seyler
Volume:386
Issue / Number:12
Start Page:1239
End Page:1252
Copyright:© Walter de Gruyter 2006
Review Status:not specified
Audience:Experts Only
Abstract / Description:In the cell, the protein synthetic machinery is a highly complex apparatus that offers many potential sites for functional interference and therefore represents a major target for antibiotics. The recent plethora of crystal structures of ribosomal subunits in complex with various antibiotics has provided unparalleled insight into their mode of interaction and inhibition. However, differences in the conformation, orientation and position of some of these drugs bound to ribosomal subunits of Deinococcus radiodurans (D50S) compared to Haloarcula marismortui (H50S) have raised questions regarding the species specificity of binding. Revisiting the structural data for the bacterial D50S-antibiotic complexes reveals that the mode of binding of the macrolides, ketolides, streptogramins and lincosamides is generally similar to that observed in the archaeal H50S structures. However, small discrepancies are observed, predominantly resulting from species-specific differences in the ribosomal proteins and rRNA constituting the drug-binding sites. Understanding how these small alterations at the binding site influence interaction with the drug will be essential for rational design of more potent inhibitors.
Free Keywords:antibiotics; drug; lincomycin; macrolides; protein synthesis; ribosome; streptogramin
Comment of the Author/Creator:Corresponding author: schluenz@molgen.mpg.de
External Publication Status:published
Document Type:Article
Communicated by:Ribosome Group
Affiliations:MPI für molekulare Genetik
Identifiers:ISSN:1431-6730
DOI:10.1515/BC.2005.141
URL:http://www.extenza-eps.com/WDG/doi/pdf/10.1515/BC....
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