AB(5) TOXINS

被引：226

作者：

MERRITT, EA ^{[1
]}

HOL, WGJ ^{[1
]}

机构：

[1] UNIV WASHINGTON, HOWARD HUGHES MED INST, SEATTLE, WA 98195 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1995年 / 5卷 / 02期

关键词：

D O I：

10.1016/0959-440X(95)80071-9

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：

Crystal structures of shiga and pertussis toxins have recently revealed a remarkable degree of structural homology among the members of the AB(5) class of bacterial toxins. Other structures have provided a detailed view of the molecular basis of receptor binding specificity of cholera toxin, and of the heat-labile enterotoxin of Escherichia coli. These structures also provide tantalizing, but as yet incomplete, information on the site of ADP-ribosylation in the homologous A-subunits of the Escherichia coli heat-labile toxin, cholera toxin, and pertussis toxin.

引用

页码：165 / 171

页数：7

共 49 条

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