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| | ==Crystal structure of FKBP25 from Plasmodium Vivax== | | ==Crystal structure of FKBP25 from Plasmodium Vivax== |
| - | <StructureSection load='4jys' size='340' side='right' caption='[[4jys]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4jys' size='340' side='right'caption='[[4jys]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4jys]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plavs Plavs]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JYS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JYS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4jys]] is a 2 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=4JYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JYS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PVX_122487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=126793 PLAVS])</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=4jys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jys OCA], [https://pdbe.org/4jys PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jys RCSB], [https://www.ebi.ac.uk/pdbsum/4jys PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jys ProSAT]</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=4jys FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jys OCA], [http://pdbe.org/4jys PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jys RCSB], [http://www.ebi.ac.uk/pdbsum/4jys PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jys ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A5JZC2_PLAVS A5JZC2_PLAVS] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Plavs]] | + | [[Category: Large Structures]] |
| - | [[Category: Sreekanth, R]] | + | [[Category: Plasmodium vivax Sal-1]] |
| - | [[Category: Yoon, H S]] | + | [[Category: Sreekanth R]] |
| - | [[Category: Fkbp]] | + | [[Category: Yoon HS]] |
| - | [[Category: Fkbp25]]
| + | |
| - | [[Category: Isomerase]]
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| - | [[Category: Non-canonical]]
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| - | [[Category: Plasmodium vivax]]
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| Structural highlights
Function
A5JZC2_PLAVS
Publication Abstract from PubMed
The malarial parasites currently remain one of the most dreadful parasites, which show increasing trend of drug resistance to the currently available antimalarial drugs. Thus, the need to identify and characterize new protein targets in these parasites can aid to design novel therapeutic strategies to combat malaria. Recently, the conserved FK506-binding protein family members with molecular weight of 35 kDa from Plasmodium falciparum and Plasmodium vivax (referred to as PfFKBP35 and PvFKBP35, respectively) were identified for drug targeting. Further data mining revealed a 25-kDa FKBP (FKBP25) family member present in the parasites. FKBP25 belongs to a unique class of FKBP, because it is a nuclear FKBP with multiple protein-binding partners. Apart from immune regulation, it is also known for its chaperoning role in various cellular processes such as transcription regulation and trafficking. Here, we present the biochemical characterization and 1.9-A crystal structure of an N-terminal truncated FKBP25 from P. vivax (PvFKBP2572-209 ). The protein reveals the noncanonical nature with unique structural changes observed in the loops flanking the active site, concealing the binding pocket. Further, a potential calmodulin-binding domain, which is absent in human FKBP25, is observed in this protein. Although the functional implication of Plasmodium FKBP25 in malaria still remains elusive, we speculate that the notable conformational changes in its structure might serve as an overture in understanding its molecular mechanism. Proteins 2013. (c) 2013 Wiley Periodicals, Inc.
Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity.,Rajan S, Austin D, Harikishore A, Nguyen QT, Baek K, Yoon HS Proteins. 2013 Dec 3. doi: 10.1002/prot.24487. PMID:24302348[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rajan S, Austin D, Harikishore A, Nguyen QT, Baek K, Yoon HS. Crystal structure of Plasmodium vivax FK506-binding protein 25 reveals conformational changes responsible for its noncanonical activity. Proteins. 2013 Dec 3. doi: 10.1002/prot.24487. PMID:24302348 doi:http://dx.doi.org/10.1002/prot.24487
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