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| | <StructureSection load='3ihz' size='340' side='right'caption='[[3ihz]], [[Resolution|resolution]] 1.67Å' scene=''> | | <StructureSection load='3ihz' size='340' side='right'caption='[[3ihz]], [[Resolution|resolution]] 1.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ihz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Haemamoeba_vivax Haemamoeba vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IHZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3IHZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ihz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_vivax Plasmodium vivax]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IHZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IHZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.67Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vn1|2vn1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FK5:8-DEETHYL-8-[BUT-3-ENYL]-ASCOMYCIN'>FK5</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ihz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ihz OCA], [http://pdbe.org/3ihz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ihz RCSB], [http://www.ebi.ac.uk/pdbsum/3ihz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ihz ProSAT]</span></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=3ihz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ihz OCA], [https://pdbe.org/3ihz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ihz RCSB], [https://www.ebi.ac.uk/pdbsum/3ihz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ihz ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A5K8X6_PLAVS A5K8X6_PLAVS] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haemamoeba vivax]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alag, R]] | |
| - | [[Category: Lescar, J]] | |
| - | [[Category: Qureshi, I A]] | |
| - | [[Category: Yoon, H S]] | |
| - | [[Category: Fk506]] | |
| - | [[Category: Fkbp35]] | |
| - | [[Category: Isomerase]] | |
| | [[Category: Plasmodium vivax]] | | [[Category: Plasmodium vivax]] |
| | + | [[Category: Alag R]] |
| | + | [[Category: Lescar J]] |
| | + | [[Category: Qureshi IA]] |
| | + | [[Category: Yoon HS]] |
| Structural highlights
Function
A5K8X6_PLAVS
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The emergence of drug-resistant malaria parasites is the major threat to effective malaria control, prompting a search for novel compounds with mechanisms of action that are different from the traditionally used drugs. The immunosuppressive drug FK506 shows an antimalarial activity. The mechanism of the drug action involves the molecular interaction with the parasite target proteins PfFKBP35 and PvFKBP35, which are novel FK506 binding protein family (FKBP) members from Plasmodium falciparum and Plasmodium vivax, respectively. Currently, molecular mechanisms of the FKBP family proteins in the parasites still remain elusive. To understand their functions, here we have determined the structures of the FK506 binding domain of Plasmodium vivax (PvFKBD) in unliganded form by NMR spectroscopy and in complex with FK506 by X-ray crystallography. We found out that PvFKBP35 exhibits a canonical FKBD fold and shares kinetic profiles similar to those of PfFKBP35, the homologous protein in P. falciparum, indicating that the parasite FKBP family members play similar biological roles in their life cycles. Despite the similarity, differences were observed in the ligand binding modes between PvFKBD and HsFKBP12, a human FKBP homolog, which could provide insightful information into designing selective antimalarial drug against the parasites.
NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35.,Alag R, Qureshi IA, Bharatham N, Shin J, Lescar J, Yoon HS Protein Sci. 2010 Aug;19(8):1577-86. PMID:20572013[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alag R, Qureshi IA, Bharatham N, Shin J, Lescar J, Yoon HS. NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35. Protein Sci. 2010 Aug;19(8):1577-86. PMID:20572013 doi:10.1002/pro.438
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