Abstract
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 Ca(2+) channels. The structure of toxin PRTx27C3 was modeled and compared with toxin ADO1. The importance of four residues is suggested.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Calcium Channel Blockers / chemistry
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Calcium Channel Blockers / isolation & purification
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Calcium Channel Blockers / toxicity
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Calcium Channels, L-Type / drug effects
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Chromatography, High Pressure Liquid
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Chromatography, Ion Exchange
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Mice
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Neurotoxins / chemistry*
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Neurotoxins / genetics
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Neurotoxins / isolation & purification
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Neurotoxins / toxicity
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Protein Conformation
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Sequence Homology, Amino Acid
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Spectrometry, Mass, Electrospray Ionization
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Spider Venoms / chemistry*
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Spider Venoms / genetics
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Spider Venoms / isolation & purification
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Spider Venoms / toxicity
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Spiders / chemistry*
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Spiders / genetics
Substances
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Calcium Channel Blockers
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Calcium Channels, L-Type
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Neurotoxins
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Spider Venoms