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==Crystal structure of FK506 binding domain of plasmodium falciparum FKBP35 in complex with D44== | ==Crystal structure of FK506 binding domain of plasmodium falciparum FKBP35 in complex with D44== | ||
<StructureSection load='4j4n' size='340' side='right' caption='[[4j4n]], [[Resolution|resolution]] 2.75Å' scene=''> | <StructureSection load='4j4n' size='340' side='right' caption='[[4j4n]], [[Resolution|resolution]] 2.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j4n]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4j4n]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Plaf7 Plaf7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J4N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J4N FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D44:N-(2-ETHYLPHENYL)-2-(3H-IMIDAZO[4,5-B]PYRIDIN-2-YLSULFANYL)ACETAMIDE'>D44</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D44:N-(2-ETHYLPHENYL)-2-(3H-IMIDAZO[4,5-B]PYRIDIN-2-YLSULFANYL)ACETAMIDE'>D44</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vn1|2vn1]], [[2ofn|2ofn]], [[4j4o|4j4o]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vn1|2vn1]], [[2ofn|2ofn]], [[4j4o|4j4o]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP35, PFL2275C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKBP35, PFL2275C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=36329 PLAF7])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=4j4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4j4n RCSB], [http://www.ebi.ac.uk/pdbsum/4j4n PDBsum]</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=4j4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4n OCA], [http://pdbe.org/4j4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j4n RCSB], [http://www.ebi.ac.uk/pdbsum/4j4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4j4n" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
| Line 25: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: | [[Category: Plaf7]] | ||
[[Category: Harikishore, A]] | [[Category: Harikishore, A]] | ||
[[Category: Sreekanth, R]] | [[Category: Sreekanth, R]] | ||
Revision as of 14:34, 11 August 2016
Crystal structure of FK506 binding domain of plasmodium falciparum FKBP35 in complex with D44Crystal structure of FK506 binding domain of plasmodium falciparum FKBP35 in complex with D44
Structural highlights
Publication Abstract from PubMedMalaria parasite strains have emerged to tolerate the therapeutic effects of the prophylactics and drugs presently available. This resistance now poses a serious challenge to researchers in the bid to overcome malaria parasitic infection. Recent studies have shown that FK520 and its analogs inhibit malaria parasites growth by binding to FK506 binding proteins (FKBPs) of the parasites. Structure based drug screening efforts based on three-dimensional structural information of FKBPs from Plasmodium falciparum led us to identify new chemical entities that bind to the parasite FKBP35 and inhibit its growth. Our experimental results verify that this novel compound (D44) modulate the PPIase activity of Plasmodium FKBP35 and demonstrate the stage-specific growth inhibition of Plasmodium falciparum strains. Here, we present the X-ray crystallographic structures of FK506 binding domains (FKBDs) of PfFKBP35 and PvFKBP35 in complex with the newly identified inhibitor providing molecular insights into its mode of action. Small molecule Plasmodium FKBP35 inhibitor as a potential antimalaria agent.,Harikishore A, Niang M, Rajan S, Preiser PR, Yoon HS Sci Rep. 2013 Aug 26;3:2501. doi: 10.1038/srep02501. PMID:23974147[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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