3eov: Difference between revisions
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<StructureSection load='3eov' size='340' side='right'caption='[[3eov]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3eov' size='340' side='right'caption='[[3eov]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3eov]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3eov]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EOV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EOV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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=3eov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eov OCA], [https://pdbe.org/3eov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eov RCSB], [https://www.ebi.ac.uk/pdbsum/3eov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eov 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=3eov FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3eov OCA], [https://pdbe.org/3eov PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3eov RCSB], [https://www.ebi.ac.uk/pdbsum/3eov PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3eov ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania donovani]] | ||
[[Category: | [[Category: Tolypocladium inflatum]] | ||
[[Category: Banerjee | [[Category: Banerjee R]] | ||
[[Category: Dasgupta | [[Category: Dasgupta D]] | ||
[[Category: Datta | [[Category: Datta AK]] | ||
[[Category: Venugopal | [[Category: Venugopal V]] | ||
Latest revision as of 09:30, 6 September 2023
Crystal structure of cyclophilin from Leishmania donovani ligated with cyclosporin ACrystal structure of cyclophilin from Leishmania donovani ligated with cyclosporin A
Structural highlights
FunctionQ9U9R3_LEIDO PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] 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 PubMedDrug development against Leishmania donovani, the pathogen that causes visceral leishmaniasis in humans, is currently an active area of research given the widespread prevalence of the disease and the emergence of resistant strains. The immunosuppressive drug cyclosporin is known to have antiparasitic activity against a variety of pathogens. The receptor for cyclosporin is the protein cyclophilin, which is a ubiquitous peptidylprolyl isomerase. The crystal structure of cyclophilin from L. donovani complexed with cyclosporin has been solved at 2.6 A resolution. The thermodynamic parameters of the interaction have been determined using spectroscopic and calorimetric techniques. A detailed effort has been made to predict the thermodynamic parameters of binding from computations based on the three-dimensional crystal structure. These results were in good agreement with the corresponding experimental values. Furthermore, the structural and biophysical results have been discussed in the context of leishmanial drug resistance and could also set the stage for the design of potent non-immunosuppressive antileishmanials. Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data.,Venugopal V, Datta AK, Bhattacharyya D, Dasgupta D, Banerjee R Acta Crystallogr D Biol Crystallogr. 2009 Nov;65(Pt 11):1187-95. Epub 2009, Oct 22. PMID:19923714[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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