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New page: left|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 2.47&Aring;" />
'''CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A'''<br />


==Overview==
==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, 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.
<StructureSection load='1c5f' size='340' side='right'caption='[[1c5f]], [[Resolution|resolution]] 2.47&Aring;' 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]] 2.47&#8491;</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.


==About this Structure==
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>
1C5F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. This structure superseeds the now removed PDB entry 1QTL. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C5F OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10642184 10642184]
</div>
<div class="pdbe-citations 1c5f" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Brugia malayi]]
[[Category: Brugia malayi]]
[[Category: Peptidylprolyl isomerase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Tolypocladium inflatum]]
[[Category: Carlow, C.K.S.]]
[[Category: Carlow CKS]]
[[Category: Ellis, P.J.]]
[[Category: Ellis PJ]]
[[Category: Kuhn, P.]]
[[Category: Kuhn P]]
[[Category: Ma, D.]]
[[Category: Ma D]]
[[Category: cyclosporin]]
[[Category: isomerase]]
[[Category: isomerase/immune system]]
[[Category: peptidyl-prolyl cis-trans]]
[[Category: peptidylprolyl isomerase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:10:23 2007''

Latest revision as of 23:23, 27 December 2023

CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A

1c5f, resolution 2.47Å

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