1x5v
From Proteopedia
NMR Structure of PcFK1
Structural highlights
FunctionNTA_PSACA Possesses strong antiplasmodial activity against the intra-erythrocyte stage of P.falciparum in vitro. IC(50) for inhibiting P.falciparum growth is 1.59 uM. Interacts with infected and healthy erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. Has neither antibacterial nor antifungal activity.[1] Publication Abstract from PubMedPsalmopeotoxin I (PcFK1) is a 33-amino-acid residue peptide isolated from the venom of the tarantula Psalmopoeus cambridgei. It has been recently shown to possess strong antiplasmodial activity against the intra-erythrocyte stage of Plasmodium falciparum in vitro. Although the molecular target for PcFK1 is not yet determined, this peptide does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neuromuscular function. We investigated the structural properties of PcFK1 to help understand the unique mechanism of action of this peptide and to enhance its utility as a lead compound for rational development of new antimalarial drugs. In this paper, we have determined the three-dimensional solution structure by (1)H two-dimensional NMR means of recombinant PcFK1, which is shown to belong to the ICK structural superfamily with structural determinants common to several neurotoxins acting as ion channels effectors. Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum.,Pimentel C, Choi SJ, Chagot B, Guette C, Camadro JM, Darbon H Protein Sci. 2006 Mar;15(3):628-34. Epub 2006 Feb 1. PMID:16452619[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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