THE CRYSTAL-STRUCTURE OF DIPHTHERIA-TOXIN
THE CRYSTAL-STRUCTURE OF DIPHTHERIA-TOXIN
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DOI：
10.1038/357216a0
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发表时间：
1992-05-21
期刊：
影响因子：
64.8
通讯作者：
EISENBERG, D
中科院分区：
文献类型：
--
作者：
CHOE, S;BENNETT, MJ;EISENBERG, D
白喉毒素二聚体在2.5埃分辨率下的晶体结构揭示了三个结构域的Y形分子。被称为片段A的催化结构域是α + β型的。片段B实际上由两个结构域组成。跨膜结构域由九个α-螺旋组成，其中两对是异常非极性的，可能参与pH触发的膜插入和易位。受体结合结构域是一个扁平的β-桶，具有卷曲样拓扑结构。毒素的三种不同功能，每种功能由单独的结构域进行，可用于设计嵌合蛋白，如免疫毒素，其中受体结合结构域被抗体取代以靶向其他细胞类型。
The crystal structure of the diphtheria toxin dimer at 2.5 angstrom resolution reveals a Y-shaped molecule of three domains. The catalytic domain, called fragment A, is of the alpha + beta-type. Fragment B actually consists of two domains. The transmembrane domain consists of nine alpha-helices, two pairs of which are unusually apolar and may participate in pH-triggered membrane insertion and translocation. The receptor-binding domain is a flattened beta-barrel with a jelly-roll-like topology. Three distinct functions of the toxin, each carried out by a separate structural domain, can be useful in designing chimaeric proteins, such as immunotoxins, in which the receptor-binding domain is substituted with antibodies to target other cell types.