1BZL
CRYSTAL STRUCTURE OF TRYPANOSOMA CRUZI TRYPANOTHIONE REDUCTASE IN COMPLEX WITH TRYPANOTHIONE, AND THE STRUCTURE-BASED DISCOVERY OF NEW NATURAL PRODUCT INHIBITORS
Summary for 1BZL
| Entry DOI | 10.2210/pdb1bzl/pdb |
| Descriptor | TRYPANOTHIONE REDUCTASE (OXIDIZED FORM), FLAVIN-ADENINE DINUCLEOTIDE, BIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE, ... (4 entities in total) |
| Functional Keywords | oxidoreductase, trypanothione reductase, fad dependent disulphide oxidoreductase |
| Biological source | Trypanosoma cruzi |
| Total number of polymer chains | 2 |
| Total formula weight | 109632.76 |
| Authors | Bond, C.S.,Zhang, Y.,Berriman, M.,Cunningham, M.,Fairlamb, A.H.,Hunter, W.N. (deposition date: 1998-11-02, release date: 1999-11-10, Last modification date: 2024-10-16) |
| Primary citation | Bond, C.S.,Zhang, Y.,Berriman, M.,Cunningham, M.L.,Fairlamb, A.H.,Hunter, W.N. Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors. Structure Fold.Des., 7:81-89, 1999 Cited by PubMed Abstract: Trypanothione reductase (TR) helps to maintain an intracellular reducing environment in trypanosomatids, a group of protozoan parasites that afflict humans and livestock in tropical areas. This protective function is achieved via reduction of polyamine-glutathione conjugates, in particular trypanothione. TR has been validated as a chemotherapeutic target by molecular genetics methods. To assist the development of new therapeutics, we have characterised the structure of TR from the pathogen Trypanosoma cruzi complexed with the substrate trypanothione and have used the structure to guide database searches and molecular modelling studies. PubMed: 10368274DOI: 10.1016/S0969-2126(99)80011-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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