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Trypanothione reductase
From Proteopedia
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<StructureSection load='4adw' size='340' side='right' caption='Trypanosoma FAD-containing trypanothione reductase dimer complex with trypanothione and NADPH [[4adw]]' scene=''> | <StructureSection load='4adw' size='340' side='right' caption='Trypanosoma FAD-containing trypanothione reductase dimer complex with trypanothione and NADPH [[4adw]]' scene=''> | ||
== Function == | == Function == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | + | The active site of TTR contains two catalytic cysteine residues which are part of the electron transfer function of the enzyme and the bound TPT substrate<ref>PMID:23733388</ref>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 10:40, 26 September 2016
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3D structures of trypanothione reductase
Updated on 26-September-2016
References
- ↑ Rivarola HW, Paglini-Oliva PA. Trypanosoma cruzi trypanothione reductase inhibitors: phenothiazines and related compounds modify experimental Chagas' disease evolution. Curr Drug Targets Cardiovasc Haematol Disord. 2002 Jun;2(1):43-52. PMID:12769656
- ↑ Baiocco P, Poce G, Alfonso S, Cocozza M, Porretta GC, Colotti G, Biava M, Moraca F, Botta M, Yardley V, Fiorillo A, Lantella A, Malatesta F, Ilari A. Inhibition of Leishmania infantum Trypanothione Reductase by Azole-Based Compounds: a Comparative Analysis with Its Physiological Substrate by X-ray Crystallography. ChemMedChem. 2013 Jun 3. doi: 10.1002/cmdc.201300176. PMID:23733388 doi:10.1002/cmdc.201300176
