1X5V

NMR Structure of PcFK1

Summary for 1X5V

• Entry DOI: 10.2210/pdb1x5v/pdb
• NMR Information: BMRB: 6636
• Descriptor: PcFK1 (1 entity in total)
• Functional Keywords: inhibitory cystine knot, toxin
• Biological source: Psalmopoeus cambridgei (Trinidad chevron tarantula)
• Cellular location: Secreted: P0C201
• Total number of polymer chains: 1
• Total formula weight: 3712.40

Authors

Pimentel, C.,Choi, S.J.,Chagot, B.,Guette, C.,Camadro, J.M.,Darbon, H. (deposition date: 2005-05-17, release date: 2006-04-04, Last modification date: 2022-03-02)

Primary citation

Pimentel, C.,Choi, S.J.,Chagot, B.,Guette, C.,Camadro, J.M.,Darbon, H.
Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum
Protein Sci., 15:628-634, 2006

PubMed Abstract: Psalmopeotoxin 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.

PubMed: 16452619
DOI: 10.1110/ps.051860606

Experimental method

SOLUTION NMR