AB(5) TOXINS
AB(5) TOXINS
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DOI：
10.1016/0959-440x(95)80071-9
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发表时间：
1995-04-01
影响因子：
6.8
通讯作者：
HOL, WGJ
中科院分区：
文献类型：
--
作者：
MERRITT, EA;HOL, WGJ
滋贺和百日咳毒素的晶体结构最近揭示了AB（5）类细菌毒素成员之间的显著程度的结构同源性。其他结构提供了霍乱毒素和大肠杆菌不耐热肠毒素受体结合特异性的分子基础的详细视图。这些结构也提供了诱人的，但还不完整的，在大肠杆菌不耐热毒素，霍乱毒素和百日咳毒素的同源A-亚基的ADP-核糖基化位点的信息。
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.