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1c5f
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1c5f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c5f, resolution 2.47Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1c5f.gif|left|200px]]<br /><applet load="1c5f" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1c5f, resolution 2.47Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A== |
| - | The resistance of the human parasite Brugia malayi to the antiparasitic | + | <StructureSection load='1c5f' size='340' side='right'caption='[[1c5f]], [[Resolution|resolution]] 2.47Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1c5f]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qtl 1qtl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C5F 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]] 2.47Å</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=1c5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5f OCA], [https://pdbe.org/1c5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c5f RCSB], [https://www.ebi.ac.uk/pdbsum/1c5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c5f ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CYP1_BRUMA CYP1_BRUMA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c5/1c5f_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c5f ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The resistance of the human parasite Brugia malayi to the antiparasitic activity of cyclosporin A (CsA) may arise from the presence of cyclophilins with relatively low affinity for the drug. The structure of the complex of B. malayi cyclophilin (BmCYP-1) and CsA, with eight independent copies in the asymmetric unit, has been determined at a resolution of 2.7 A. The low affinity of BmCYP-1 for CsA arises from incomplete preorganization of the binding site so that the formation of a hydrogen bond between His132 of BmCYP-1 and N-methylleucine 9 of CsA is associated with a shift in the backbone of approximately 1 A in this region. | ||
| - | + | Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.,Ellis PJ, Carlow CK, Ma D, Kuhn P Biochemistry. 2000 Jan 25;39(3):592-8. PMID:10642184<ref>PMID:10642184</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1c5f" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Brugia malayi]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tolypocladium inflatum]] | ||
| + | [[Category: Carlow CKS]] | ||
| + | [[Category: Ellis PJ]] | ||
| + | [[Category: Kuhn P]] | ||
| + | [[Category: Ma D]] | ||
Current revision
CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A
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