Polypeptide neurotoxins from spider venoms

被引：71

作者：

Grishin, E ^{[1
]}

机构：

[1] Russian Acad Sci, Shemyakin Ovchinnikov Inst Bioorgan Chem, Moscow 117871, Russia

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1999年 / 264卷 / 02期

关键词：

spider venom toxins; polypeptide toxins; amino acid sequence; spatial structure; cation channels; latrotoxins; neurotransmitter release; gene cloning;

D O I：

10.1046/j.1432-1327.1999.00622.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：276 / 280

页数：5

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