2ck1: Difference between revisions
New page: left|200px<br /> <applet load="2ck1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ck1, resolution 1.80Å" /> '''THE STRUCTURE OF OX... |
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==About this Structure== | ==About this Structure== | ||
2CK1 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]] with ACT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=2CK1 OCA]]. | 2CK1 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Schistosoma_mansoni Schistosoma mansoni]] with ACT as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CK1 OCA]]. | ||
==Reference== | ==Reference== | ||
The three-dimensional structure of two redox states of cyclophilin-A from schistosoma mansoni: Evidence for redox- regulation of peptidyl-prolyl cis-trans isomerase activity., Gourlay LJ, Angelucci F, Baiocco P, Boumis G, Brunori M, Bellelli A, Miele AE, J Biol Chem. 2007 Jun 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17591771 17591771] | The three-dimensional structure of two redox states of cyclophilin-A from schistosoma mansoni: Evidence for redox- regulation of peptidyl-prolyl cis-trans isomerase activity., Gourlay LJ, Angelucci F, Baiocco P, Boumis G, Brunori M, Bellelli A, Miele AE, J Biol Chem. 2007 Jun 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17591771 17591771] | ||
[[Category: Peptidylprolyl isomerase]] | |||
[[Category: Schistosoma mansoni]] | [[Category: Schistosoma mansoni]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rotamase activity]] | [[Category: rotamase activity]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:35:32 2007'' | ||
Revision as of 15:30, 30 October 2007
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THE STRUCTURE OF OXIDISED CYCLOPHILIN A FROM S. MANSONI
OverviewOverview
Treatment of Schistosomiasis, a widespread human parasitic disease caused, by the helminth parasites of the genus Schistosoma, relies mainly on one, chemotherapeutic agent, praziquantel, although several other compounds, exert anti-parasitic effects. One such compound is the immunosuppressant, cyclosporin A, which has been shown to significantly diminish worm burden, in mice infected with S. mansoni. Given the well-established interaction, between cyclosporin A and the cyclophilin superfamily of peptidyl-prolyl, cis-trans isomerases, we solved the structure of cyclophilin A from S., mansoni (SmCypA) by X-ray crystallography in the reduced and oxidised, states, at 1.5A and 1.8A resolution respectively. Oxidised SmCypA contains, a disulphide bridge between two C-terminal cysteines (C122 and ... [(full description)]
About this StructureAbout this Structure
2CK1 is a [Single protein] structure of sequence from [Schistosoma mansoni] with ACT as [ligand]. Active as [Peptidylprolyl isomerase], with EC number [5.2.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The three-dimensional structure of two redox states of cyclophilin-A from schistosoma mansoni: Evidence for redox- regulation of peptidyl-prolyl cis-trans isomerase activity., Gourlay LJ, Angelucci F, Baiocco P, Boumis G, Brunori M, Bellelli A, Miele AE, J Biol Chem. 2007 Jun 25;. PMID:17591771
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