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  Species-specific antibiotic-ribosome interactions: implications for drug development

Wilson, D. N., Harms, J. M., Nierhaus, K. H., Schlünzen, F., & Fucini, P. (2005). Species-specific antibiotic-ribosome interactions: implications for drug development. Biological Chemistry Hoppe-Seyler (Berlin), 386(12), 1239-1252. doi:10.1515/BC.2005.141.

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Datensatz-Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8548-5 Versions-Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8549-3
Genre: Zeitschriftenartikel
Alternativer Titel : Biol Chem Hoppe Seyler

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 Urheber:
Wilson, Daniel N.1, Autor              
Harms, Jörg M.2, Autor
Nierhaus, Knud H.3, Autor              
Schlünzen, Frank2, Autor
Fucini, Paola3, Autor              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, escidoc:1433550              
2Max Planck Society, escidoc:persistent13              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, escidoc:1433558              

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Schlagwörter: antibiotics; drug; lincomycin; macrolides; protein synthesis; ribosome; streptogramin
 Zusammenfassung: 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.

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Sprache(n): eng - Englisch
 Datum: 2005-12
 Publikationsstatus: Im Druck publiziert
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Art des Abschluß: -

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Titel: Biological Chemistry Hoppe-Seyler (Berlin)
  Alternativer Titel : Biol Chem Hoppe Seyler
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: 386 (12) Artikelnummer: - Start- / Endseite: 1239 - 1252 Identifikator: ISSN: 1431-6730