4fh8
From Proteopedia
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| - | + | ==Crystal Structure of Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum== | |
| - | + | <StructureSection load='4fh8' size='340' side='right' caption='[[4fh8]], [[Resolution|resolution]] 2.11Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4fh8]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Ancylostoma_ceylanicum Ancylostoma ceylanicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FH8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FH8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fh9|4fh9]], [[3tjb|3tjb]], [[1qmv|1qmv]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peroxiredoxin Peroxiredoxin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.15 1.11.1.15] </span></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fh8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fh8 RCSB], [http://www.ebi.ac.uk/pdbsum/4fh8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hookworms are parasitic nematodes that have a devastating impact on global health, particularly in developing countries. We report a biochemical and structural analysis of a peroxiredoxin from the hookworm Ancylostoma ceylanicum, AcePrx-1. Peroxiredoxins provide antioxidant protection and act as signaling molecules and chaperones. AcePrx-1 is expressed in adult hookworms and can be inactivated by 2,3-bis(bromomethyl)quinoxaline-1,4-dioxide (conoidin A). Conoidin A inactivates AcePrx-1 by alkylating or crosslinking the catalytic cysteines, while maintaining the enzyme in the "locally unfolded" conformation. Irreversible oxidation of the resolving cysteine may contribute additional inhibitory activity. A crystal structure of oxidized AcePrx-1 reveals a disulfide-linked decamer. A helix macrodipole near the active site increases the reactivity of the catalytic cysteines to conoidin A. This work demonstrates the promise of conoidin compounds as probes to evaluate peroxiredoxins as drug targets in human parasites. | ||
| - | + | Peroxiredoxin-1 from the Human Hookworm Ancylostoma ceylanicum Forms a Stable Oxidized Decamer and Is Covalently Inhibited by Conoidin A.,Nguyen JB, Pool CD, Wong CY, Treger RS, Williams DL, Cappello M, Lea WA, Simeonov A, Vermeire JJ, Modis Y Chem Biol. 2013 Jul 23. pii: S1074-5521(13)00244-5. doi:, 10.1016/j.chembiol.2013.06.011. PMID:23891152<ref>PMID:23891152</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | |||
| + | ==See Also== | ||
| + | *[[Peroxiredoxin|Peroxiredoxin]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ancylostoma ceylanicum]] | [[Category: Ancylostoma ceylanicum]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
| - | [[Category: Modis, Y | + | [[Category: Modis, Y]] |
| - | [[Category: Nguyen, J B | + | [[Category: Nguyen, J B]] |
[[Category: 2-cys peroxiredoxin]] | [[Category: 2-cys peroxiredoxin]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 11:35, 21 December 2014
Crystal Structure of Peroxiredoxin-1 from the human hookworm Ancylostoma ceylanicum
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