1c5f
From Proteopedia
(Difference between revisions)
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- | + | ==CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A== | |
- | + | <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 [http://en.wikipedia.org/wiki/Brugia_malayi Brugia malayi]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1C5F FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bck|1bck]], [[1csa|1csa]], [[1cwa|1cwa]], [[1cwb|1cwb]], [[1cwc|1cwc]], [[1cwf|1cwf]], [[1cwh|1cwh]], [[1cwi|1cwi]], [[1cwj|1cwj]], [[1cwk|1cwk]], [[1cwl|1cwl]], [[1cwm|1cwm]], [[1cwo|1cwo]], [[1cya|1cya]], [[1cyb|1cyb]], [[1cyn|1cyn]], [[1ikf|1ikf]], [[1m63|1m63]], [[1mf8|1mf8]], [[1mik|1mik]], [[1qng|1qng]], [[1qnh|1qnh]], [[1xq7|1xq7]], [[2esl|2esl]], [[2oju|2oju]], [[2poy|2poy]], [[2rma|2rma]], [[2rmb|2rmb]], [[2rmc|2rmc]], [[2wfj|2wfj]], [[2x2c|2x2c]], [[2x7k|2x7k]], [[2z6w|2z6w]], [[3bo7|3bo7]], [[3cys|3cys]], [[3eov|3eov]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMCYP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6279 Brugia malayi])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c5f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1c5f RCSB], [http://www.ebi.ac.uk/pdbsum/1c5f PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | == 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/chain_selection.php?pdb_ID=2ata 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> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Brugia malayi]] | [[Category: Brugia malayi]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] |
Revision as of 08:47, 3 October 2014
CRYSTAL STRUCTURE OF THE CYCLOPHILIN-LIKE DOMAIN FROM BRUGIA MALAYI COMPLEXED WITH CYCLOSPORIN A
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