4j4o: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of FK506 binding domain of plasmodium VIVAX FKBP35 in complex with D44== | |||
<StructureSection load='4j4o' size='340' side='right'caption='[[4j4o]], [[Resolution|resolution]] 1.73Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4j4o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax_Sal-1 Plasmodium vivax Sal-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J4O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J4O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.73Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D44:N-(2-ETHYLPHENYL)-2-(3H-IMIDAZO[4,5-B]PYRIDIN-2-YLSULFANYL)ACETAMIDE'>D44</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4j4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j4o OCA], [https://pdbe.org/4j4o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j4o RCSB], [https://www.ebi.ac.uk/pdbsum/4j4o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j4o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5K8X6_PLAVS A5K8X6_PLAVS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Malaria 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<ref>PMID:23974147</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4j4o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium vivax Sal-1]] | |||
[[Category: Harikishore A]] | |||
[[Category: Sreekanth R]] | |||
[[Category: Yoon HS]] | |||
Latest revision as of 17:20, 8 November 2023
Crystal structure of FK506 binding domain of plasmodium VIVAX FKBP35 in complex with D44Crystal structure of FK506 binding domain of plasmodium VIVAX FKBP35 in complex with D44
Structural highlights
FunctionPublication 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. References
|
| ||||||||||||||||||