Fig. 1.
Fig. 1. Alignment of the putative plasmodial sequence with the sequences for human IRPs. / (A) Sequence comparison of PfIRPa with human IRP1 and IRP2. On the basis of the comparison with the mitochondrial porcine aconitase,30 the critical residues for substrate recognition, catalysis, cluster ligation and interaction, and hydrogen bond support are shown. The alignment was performed using the program ClustalW (Baylor College of Medicine, Houston, TX). (B) Schematic comparison of PfIRPa with human IRP1 and IRP2. Active site residues that are shared among the IRPs are shown within each domain.32 Active site residues that differ are shown in bold type. The alignment and sequence conservation is high among the 3 proteins.

Alignment of the putative plasmodial sequence with the sequences for human IRPs.

(A) Sequence comparison of PfIRPa with human IRP1 and IRP2. On the basis of the comparison with the mitochondrial porcine aconitase,30 the critical residues for substrate recognition, catalysis, cluster ligation and interaction, and hydrogen bond support are shown. The alignment was performed using the program ClustalW (Baylor College of Medicine, Houston, TX). (B) Schematic comparison of PfIRPa with human IRP1 and IRP2. Active site residues that are shared among the IRPs are shown within each domain.32 Active site residues that differ are shown in bold type. The alignment and sequence conservation is high among the 3 proteins.

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