2cmt
From Proteopedia
(New page: 200px<br /> <applet load="2cmt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cmt, resolution 1.50Å" /> '''THE STRUCTURE OF RE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2CMT 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=2CMT OCA]]. | + | 2CMT 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=2CMT 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: schistosoma]] | [[Category: schistosoma]] | ||
| - | ''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 13:08:47 2007'' |
Revision as of 11:04, 30 October 2007
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THE STRUCTURE OF REDUCED CYCLOPHILIN A FROM S. MANSONI
Overview
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 Structure
2CMT 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].
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:17591771
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