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Solution structure of the <Emphasis Type="Italic">Legionella pneumophila</Emphasis> Mip-rapamycin complex |
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| Authors: | Andreas Ceymann Martin Horstmann Philipp Ehses Kristian Schweimer Anne-Katrin Paschke Michael Steinert Cornelius Faber |
| Institution: | 1.Department of Experimental Physics 5,University of Würzburg,Würzburg,Germany;2.Department of Biopolymers,University of Bayreuth,Bayreuth,Germany;3.Max Planck Research Unit "Enzymology of Protein Folding",Halle,Germany;4.Institute for Molecular Biology of Infections,University of Würzburg,Würzburg,Germany;5.Institute Virion\Serion GmbH,Würzburg,Germany;6.Department of Microbiology,Technical University of Braunschweig,Braunschweig,Germany |
| Abstract: | BackgroundLegionella pneumphila is the causative agent of Legionnaires' disease. A major virulence factor of the pathogen is the homodimeric surface protein Mip. It shows peptidyl-prolyl cis/trans isomerase activty and is a receptor of FK506 and rapamycin, which both inhibit its enzymatic function. Insight into the binding process may be used for the design of novel Mip inhibitors as potential drugs against Legionnaires' disease. |
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