2haq: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2haq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HAQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[2haq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HAQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HAQ FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5661 Leishmania donovani])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5661 Leishmania donovani])</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 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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2haq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2haq RCSB], [http://www.ebi.ac.uk/pdbsum/2haq PDBsum]</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=2haq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2haq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2haq RCSB], [http://www.ebi.ac.uk/pdbsum/2haq PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Leishmania donovani]] | [[Category: Leishmania donovani]] | ||
[[Category: Peptidylprolyl isomerase]] | [[Category: Peptidylprolyl isomerase]] | ||
[[Category: Banerjee., R | [[Category: Banerjee., R]] | ||
[[Category: Datta, A K | [[Category: Datta, A K]] | ||
[[Category: Sen, B | [[Category: Sen, B]] | ||
[[Category: Venugopal, V | [[Category: Venugopal, V]] | ||
[[Category: Cis-tran]] | [[Category: Cis-tran]] | ||
[[Category: Cyclophilin]] | [[Category: Cyclophilin]] | ||
[[Category: Donovani]] | [[Category: Donovani]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Kala-azar | [[Category: Kala-azar]] | ||
[[Category: Leishmania]] | [[Category: Leishmania]] | ||
[[Category: Proline]] | [[Category: Proline]] | ||
[[Category: Protozoa]] | [[Category: Protozoa]] | ||
[[Category: Rotamase]] | [[Category: Rotamase]] | ||
Revision as of 11:55, 16 January 2015
Crystal Structure of Cyclophilin A from Leishmania DonovaniCrystal Structure of Cyclophilin A from Leishmania Donovani
Structural highlights
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 PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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