3ul3: Difference between revisions
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<StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91Å' scene=''> | <StructureSection load='3ul3' size='340' side='right'caption='[[3ul3]], [[Resolution|resolution]] 2.91Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ul3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ul3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UL3 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAL13P1.225, trx2 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAL13P1.225, trx2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ul3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ul3 OCA], [https://pdbe.org/3ul3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ul3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ul3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ul3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Thioredoxin|Thioredoxin]] | *[[Thioredoxin 3D structures|Thioredoxin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:44, 20 July 2022
Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machineryStructural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery
Structural highlights
Publication Abstract from PubMedThioredoxins are vital components of Plasmodium proteome and act as both reducing agents and protein disulfide reductases. The malaria parasite P. falciparum thioredoxin-2 (PfTrx-2) is part of the multi-protein complex embedded within the parasite parasitophorous vacuolar membrane (PVM) which purportedly directs protein secretion. We have characterized structural and enzymatic features of PfTrx-2, and we show that PfTrx-2 adopts a canonical thioredoxin fold but with significant structural differences in its N-terminus. Our confocal localization data suggest distinct PVM residency of PfTrx-2. Based on the crystal structure of PfTrx-2, we screened and tested small molecule drug-like libraries for compounds which target unique structural features of PfTrx-2. Disruption of PfTrx-2 interactions using specific inhibitors may result in a dysfunctional parasite translocon that is rendered unable to secrete pathogenic proteins into hosts. This approach therefore offers a new focus for anti-malarial drug development. Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery.,Sharma A, Sharma A, Dixit S, Sharma A Sci Rep. 2011;1:179. doi: 10.1038/srep00179. Epub 2011 Dec 1. PMID:22355694[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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