Protein and Peptide Letters · 2008 · 11 citations · 0 references
Life SciencesNeurosciencePharmacologyStructural BiochemistryStructural BioinformaticsStructural BiologyNeurotoxic MechanismsVenom BiologyReptile Venom BiologySnake Venom ToxicologyToxin BiochemistryToxin CharacterizationToxin IdentificationToxin StructureVenom Pharmacology
A family of 4kDa neurotoxic peptides was purified from venoms of Phoneutria spiders. All have six cysteine residues, and low similarity with other neurotoxins. Three toxins caused moderate inhibition of L-type Ca2+ channels. The structure of toxin PRTx27C3 was modeled and compared with toxin ADO1. The importance of four residues is suggested. Keywords: Spider toxin, neurotoxin, Phoneutria, amino acid sequences, L-type Ca 2+ channels, molecular modeling