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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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アイテムのパーマリンク: http://hdl.handle.net/11858/00-001M-0000-0010-8548-5 版のパーマリンク: http://hdl.handle.net/11858/00-001M-0000-0010-8549-3
資料種別: 学術論文
その他のタイトル : Biol Chem Hoppe Seyler

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 作成者:
Wilson, Daniel N.1, 著者              
Harms, Jörg M.2, 著者
Nierhaus, Knud H.3, 著者              
Schlünzen, Frank2, 著者
Fucini, Paola3, 著者              
所属:
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              

内容説明

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キーワード: antibiotics; drug; lincomycin; macrolides; protein synthesis; ribosome; streptogramin
 要旨: 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.

資料詳細

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言語: eng - 英語
 日付: 2005-12
 出版の状態: 紙媒体で出版済み
 ページ: -
 出版情報: -
 目次: -
 査読: -
 学位: -

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出版物 1

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出版物名: Biological Chemistry Hoppe-Seyler (Berlin)
  出版物の別名 : Biol Chem Hoppe Seyler
種別: 学術雑誌
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出版社, 出版地: -
ページ: - 巻号: 386 (12) 通巻号: - 開始・終了ページ: 1239 - 1252 識別子(ISBN, ISSN, DOIなど): ISSN: 1431-6730