Publications by authors named "Irwin Hirsh"
Article Synopsis
- An altered version of peptide deformylase from Plasmodium falciparum has been successfully cocrystallized with a synthesized inhibitor, revealing a strong binding affinity.
- The new crystal structure is determined at 2.2 A resolution, which is an improvement over the previous 2.8 A resolution of the unliganded PfPDF, thanks to modifications made to the protein construct.
- This study presents the first-ever structure of a eukaryotic PDF protein in complex with a ligand, highlighting its potential as a drug target for malaria treatment.
Peptide deformylase catalyzes the deformylation reaction of the amino terminal fMet residue of newly synthesized proteins in bacteria, and most likely in Plasmodium falciparum, and has therefore been identified as a potential antibacterial and antimalarial drug target. The structure of P. falciparum peptide deformylase, determined at 2.
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