Polypeptide neurotoxins from spider venoms.
Spider venoms contain a variety of toxic components. The polypeptide toxins are divided into low and high molecular mass types. Small polypeptide toxins interacting with cation channels display spatial structure homology. They can affect the functioning of calcium, sodium, or potassium channels. A family of high molecular mass toxic proteins was found in the venom of the spider genus Latrodectus. These neurotoxins, latrotoxins, cause a massive transmitter release from a diversity of nerve endings. The latrotoxins are proteins of about 1000 amino acid residues and share a high level of structure identity. The structural and functional properties of spider polypeptide toxins are reviewed in this paper.
Grishin
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Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia.
D000595:Amino Acid Sequence; D000818:Animals; D007473:Ion Channels / Q000037:antagonists & inhibitors / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009498:Neurotoxins / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013111:Spider Venoms / Q000737:chemistry*
D007473:Ion Channels; D009498:Neurotoxins; D010455:Peptides; D013111:Spider Venoms