4pd4

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pd4 RCSB], [http://www.ebi.ac.uk/pdbsum/4pd4 PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pd4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pd4 RCSB], [http://www.ebi.ac.uk/pdbsum/4pd4 PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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Atovaquone, a substituted hydroxynaphthoquinone, is a potent antimalarial drug that acts by inhibiting the parasite's mitochondrial cytochrome bc1 complex (cyt bc1). Mutations in cyt bc1 confer atovaquone resistance. Here we describe the X-ray structure of mitochondrial cyt bc1 from Saccharomyces cerevisiae with atovaquone bound in the catalytic Qo site, at 3.0-A resolution. A polarized H-bond to His181 of the Rieske protein in cyt bc1 traps the ionized hydroxyl group of the drug. Side chains of highly conserved cytochrome b residues establish multiple non-polar interactions with the napththoquinone group, whereas less-conserved residues are in contact with atovaquone's cyclohexyl-chlorophenyl tail. Our structural analysis reveals the molecular basis of atovaquone's broad target spectrum, species-specific efficacies and acquired resistances, and may aid drug development to control the spread of resistant parasites.
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Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action.,Birth D, Kao WC, Hunte C Nat Commun. 2014 Jun 4;5:4029. doi: 10.1038/ncomms5029. PMID:24893593<ref>PMID:24893593</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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Revision as of 05:27, 18 June 2014

Structural analysis of atovaquone-inhibited cytochrome bc1 complex reveals the molecular basis of antimalarial drug action

4pd4, resolution 3.04Å

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