2cmt
From Proteopedia
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Revision as of 15:08, 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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