ArticleActa crystallographica. Section F, Structural biology and crystallization communications2011
Structure of recombinant Leishmania donovani pteridine reductase reveals a disordered active site.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Drug Repurposing for Kala-Azar.Pharmaceutics · 2025Article
- Structure and dynamics of pteridine reductase 1: the key phenomena relevant to enzyme function and drug design.European biophysics journal : EBJ · 2023Review
- Exploring actinomycetes natural products to identify potential multi-target inhibitors against3 Biotech · 2022Article
- Leishmanicidal Potential of Hardwickiic Acid Isolated FromFrontiers in pharmacology · 2020Article
- Dual and selective inhibitors of pteridine reductase 1 (PTR1) and dihydrofolate reductase-thymidylate synthase (DHFR-TS) fromJournal of enzyme inhibition and medicinal chemistry · 2019Article
- Exploiting the 2-Amino-1,3,4-thiadiazole Scaffold To InhibitACS omega · 2017Article
- Chroman-4-One Derivatives Targeting Pteridine Reductase 1 and Showing Anti-Parasitic Activity.Molecules (Basel, Switzerland) · 2017Article
- The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.Molecules (Basel, Switzerland) · 2016Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Pteridine reductase (PTR1) is a potential target for drug development against parasitic Trypanosoma and Leishmania species, protozoa that are responsible for a range of serious diseases found in tropical and subtropical parts of the world. As part of a structure-based approach to inhibitor development, specifically targeting Leishmania species, well ordered crystals of L. donovani PTR1 were sought to support the characterization of complexes formed with inhibitors. An efficient system for recombinant protein production was prepared and the enzyme was purified and crystallized in an orthorhombic form with ammonium sulfate as the precipitant. Diffraction data were measured to 2.5 Å resolution and the structure was solved by molecular replacement. However, a sulfate occupies a phosphate-binding site used by NADPH and occludes cofactor binding. The nicotinamide moiety is a critical component of the active site and without it this part of the structure is disordered. The crystal form obtained under these conditions is therefore unsuitable for the characterization of inhibitor complexes.
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