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2000
Volume 17, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

A three-dimensional model of the malarial drug target protein PfDXR was generated, and validated using structure-checking programs and protein docking studies. Structural and functional features unique to PfDXR were identified using the model and comparative sequence analyses with apicomplexan and non-apicomplexan DXR proteins. Furthermore, we have used the model to develop an efficient approach to screen for potential tool compounds for use in the rational design of novel DXR inhibitors.

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/content/journals/ppl/10.2174/092986610789909548
2010-01-01
2025-06-12
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/content/journals/ppl/10.2174/092986610789909548
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  • Article Type:
    Research Article
Keyword(s): antimalarial; apicomplexan; binding affinity; fosmidomycin; IC50; inhibitors; PfDXR
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