MOLECULAR DISSECTION OF CHOLINERGIC BINDING-SITES - HOW DO SNAKES ESCAPE THE EFFECT OF THEIR OWN TOXINS

被引：29

作者：

OHANA, B

FRAENKEL, Y

NAVON, G

GERSHONI, JM

机构：

[1] TEL AVIV UNIV,DEPT CELL RES & IMMUNOL,IL-69978 TEL AVIV,ISRAEL

[2] TEL AVIV UNIV,SCH CHEM,IL-69978 TEL AVIV,ISRAEL

[3] WEIZMANN INST SCI,DEPT BIOPHYS,IL-76100 REHOVOT,ISRAEL

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 179卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)91421-8

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：

Snakes have evolved a novel binding site demonstrating selective biorecognition. The snake nicotinic acetylcholine receptor is sensitive to acetylcholine while resistant to the effect of the lethal neurotoxins secreted in their own venom. By subjecting recombinant binding sites to point mutagenesis, biochemical analyses and NMR spectroscopy the binding characteristics of three cholinergic ligands have been measured. The amino acid residue at position 189 has been found to be of particular importance to toxin binding. © 1991.

引用

页码：648 / 654

页数：7

共 18 条

[1]

ARONHEIM A, 1988, J BIOL CHEM, V263, P9933

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