Abstract:
:The crystal structure of the diphtheria toxin dimer at 2.5 A 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.
journal_name
Naturejournal_title
Natureauthors
Choe S,Bennett MJ,Fujii G,Curmi PM,Kantardjieff KA,Collier RJ,Eisenberg Ddoi
10.1038/357216a0keywords:
subject
Has Abstractpub_date
1992-05-21 00:00:00pages
216-22issue
6375eissn
0028-0836issn
1476-4687journal_volume
357pub_type
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