1X5V

NMR Structure of PcFK1

1X5V の概要

• エントリーDOI: 10.2210/pdb1x5v/pdb
• NMR情報: BMRB: 6636
• 分子名称: PcFK1 (1 entity in total)
• 機能のキーワード: inhibitory cystine knot, toxin
• 由来する生物種: Psalmopoeus cambridgei (Trinidad chevron tarantula)
• 細胞内の位置: Secreted: P0C201
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3712.40

構造登録者

Pimentel, C.,Choi, S.J.,Chagot, B.,Guette, C.,Camadro, J.M.,Darbon, H. (登録日: 2005-05-17, 公開日: 2006-04-04, 最終更新日: 2022-03-02)

主引用文献

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

実験手法

SOLUTION NMR