2003
DOI: 10.1046/j.1432-1033.2003.03580.x
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Interaction of the P‐type cardiotoxin with phospholipid membranes

Abstract: The cardiotoxin (cytotoxin II, or CTII) isolated from cobra snake (Naja oxiana) venom is a 60-residue basic membraneactive protein featuring three-finger beta sheet fold. To assess possible modes of CTII/membrane interaction 31 P-and 1 H-NMR spectroscopy was used to study binding of the toxin and its effect onto multilamellar vesicles (MLV) composed of either zwitterionic or anionic phospholipid, dipalmitoylglycerophosphocholine (Pam 2 Gro-PCho) or dipalmitoylglycerophosphoglycerol (Pam 2 Gro-PGro), respective… Show more

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Cited by 40 publications
(37 citation statements)
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“…The differences in amino acids are in the three loop regions. CTX M1 and CTX M3 have proline at position 30, and therefore, they belong to the P-type cytotoxins, while CTX M4 has SER 28 and can be classified as an S-type cytotoxin [11]. The differences in amino acid residues suggest the functional diversity of these polypeptides.…”
Section: Resultsmentioning
confidence: 99%
“…The differences in amino acids are in the three loop regions. CTX M1 and CTX M3 have proline at position 30, and therefore, they belong to the P-type cytotoxins, while CTX M4 has SER 28 and can be classified as an S-type cytotoxin [11]. The differences in amino acid residues suggest the functional diversity of these polypeptides.…”
Section: Resultsmentioning
confidence: 99%
“…Influence of CTII on thermotropic properties of anionic phospholipid membranes was determined earlier [7]. Formation of an isotropic phase occurs when the lipid/protein ratio exceeds a threshold value [12]. Spatial structure of this toxin has been determined in aqueous solution [11] and in detergent micelles [9].…”
Section: Introductionmentioning
confidence: 99%
“…However, the similarity with other groups of 3FTxs, such as neurotoxins, muscarinic toxins, fasciculin, FS2 or dendroaspin, is relatively low (Figure 2B, Table 2). The P-type cardiotoxins bind to phospholipids and perturb the membrane surface with their lipid binding sites (6–13, 24–37 and 46–50 amino acid positions in the tip of loop I, II and III, respectively) [67]–[69]. These hydrophobic residues flanked by cationic residues form cytolytic region in cardiotoxins [70], [71].…”
Section: Discussionmentioning
confidence: 99%