ArticleMolecular and biochemical parasitology2013
Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.
Article in Molecular and biochemical parasitology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 29 citations in OpenAlex.
- ATP mimetics targeting prolyl-tRNA synthetases as a new avenue for antimalarial drug development.iScience · 2024Article
- Targeting prolyl-tRNA synthetase via a series of ATP-mimetics to accelerate drug discovery against toxoplasmosis.PLoS pathogens · 2023Article
- Structural analyses of the malaria parasite aminoacyl-tRNA synthetases provide new avenues for antimalarial drug discovery.Protein science : a publication of the Protein Society · 2021Review
- MalDA, Accelerating Malaria Drug Discovery.Trends in parasitology · 2021Review
- Antimalarial Properties of Isoquinoline Derivative fromBioMed research international · 2020Article
- Conformational heterogeneity in apo and drug-bound structures of Toxoplasma gondii prolyl-tRNA synthetase.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study.Malaria journal · 2019Article
- Inverse docking based screening and identification of protein targets for Cassiarin alkaloids againstSaudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2018Article
- 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
- Selective inhibition of apicoplast tryptophanyl-tRNA synthetase causes delayed death in Plasmodium falciparum.Scientific reports · 2016Article
- Recent advances in the biology and drug targeting of malaria parasite aminoacyl-tRNA synthetases.Malaria journal · 2016Review
- Novel and unique domains in aminoacyl-tRNA synthetases from human fungal pathogens Aspergillus niger, Candida albicans and Cryptococcus neoformans.BMC genomics · 2014Article
- Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase.Journal of structural and functional genomics · 2014Article
- Comparison of histidine recognition in human and trypanosomatid histidyl-tRNA synthetases.Biochimie · 2014Article
- Structural basis of malaria parasite lysyl-tRNA synthetase inhibition by cladosporin.Journal of structural and functional genomics · 2014Article
- Aminoacyl-tRNA synthetases as drug targets in eukaryotic parasites.International journal for parasitology. Drugs and drug resistance · 2014Review
- A nondiscriminating glutamyl-tRNA synthetase in the plasmodium apicoplast: the first enzyme in an indirect aminoacylation pathway.The Journal of biological chemistry · 2013Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Malaria, most commonly caused by the parasite Plasmodium falciparum, is a devastating disease that remains a large global health burden. Lack of vaccines and drug resistance necessitate the continual development of new drugs and exploration of new drug targets. Due to their essential role in protein synthesis, aminoacyl-tRNA synthetases are potential anti-malaria drug targets. Here we report the crystal structures of P. falciparum cytosolic tryptophanyl-tRNA synthetase (Pf-cTrpRS) in its ligand-free state and tryptophanyl-adenylate (WAMP)-bound state at 2.34 Å and 2.40 Å resolutions, respectively. Large conformational changes are observed when the ligand-free protein is bound to WAMP. Multiple residues, completely surrounding the active site pocket, collapse onto WAMP. Comparison of the structures to those of human cytosolic TrpRS (Hs-cTrpRS) provides information about the possibility of targeting Pf-cTrpRS for inhibitor development. There is a high degree of similarity between Pf-cTrpRS and Hs-cTrpRS within the active site. However, the large motion that Pf-cTrpRS undergoes during transitions between different functional states avails an opportunity to arrive at compounds which selectively perturb the motion, and may provide a starting point for the development of new anti-malaria therapeutics.
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