6l2b: Difference between revisions
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==Crystal structure of cyclophilin mutant I164M from Leishmania donovani at 2.65 angstrom resolution== | |||
<StructureSection load='6l2b' size='340' side='right'caption='[[6l2b]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6l2b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L2B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6L2B FirstGlance]. <br> | |||
</td></tr><tr id='activity'><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 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=6l2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l2b OCA], [http://pdbe.org/6l2b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6l2b RCSB], [http://www.ebi.ac.uk/pdbsum/6l2b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6l2b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of cyclophilin from Leishmania donovani (LdCyp) has been determined and refined at 1.97 A resolution to a crystallographic R factor of 0.178 (R(free) = 0.197). The structure was solved by molecular replacement using cyclophilin from Trypanosoma cruzi as the search model. LdCyp exhibits complete structural conservation of the cyclosporin-binding site with respect to the homologous human protein, as anticipated from LdCyp-cyclosporin binding studies. Comparisons with other cyclophilins show deviations primarily in the loop regions. The solvent structure encompassing the molecule has also been analyzed in some detail. | |||
Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.,Venugopal V, Sen B, Datta AK, Banerjee R Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt, 2):60-4. Epub 2007 Jan 17. PMID:17277440<ref>PMID:17277440</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6l2b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Peptidylprolyl isomerase]] | |||
[[Category: Banerjee, R]] | [[Category: Banerjee, R]] | ||
[[Category: Biswas, G]] | [[Category: Biswas, G]] | ||
[[Category: Datta, A K]] | |||
[[Category: Ghosh, S]] | [[Category: Ghosh, S]] | ||
[[Category: Cyclophilin]] | |||
[[Category: Isomerase]] | |||
[[Category: Peptidyl prolyl isomerase]] | |||
