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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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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8548-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-8549-3
Genre: Journal Article
Alternative Title : Biol Chem Hoppe Seyler

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 Creators:
Wilson, Daniel N.1, Author              
Harms, Jörg M.2, Author
Nierhaus, Knud H.3, Author              
Schlünzen, Frank2, Author
Fucini, Paola3, Author              
Affiliations:
1Dept. of Vertebrate Genomics (Head: Hans Lehrach), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433550              
2Max Planck Society, ou_persistent13              
3Ribosomes, Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1433558              

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Free keywords: antibiotics; drug; lincomycin; macrolides; protein synthesis; ribosome; streptogramin
 Abstract: 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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Language(s): eng - English
 Dates: 2005-12
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

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Title: Biological Chemistry Hoppe-Seyler (Berlin)
  Alternative Title : Biol Chem Hoppe Seyler
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 386 (12) Sequence Number: - Start / End Page: 1239 - 1252 Identifier: ISSN: 1431-6730