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Cited by 158

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The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core.

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Drenth, J., Low, B.W., Richardson, J.S., Wright, C.S.·1980·Journal of Biological Chemistry

Abstract

The three-dimensional structures of the snake venom postsynaptic neurotoxins and of the domains in wheat germ agglutinin show a remarkably similar overall folding pattern, consisting of equivalently placed, but variably sized loops which are held together by four similarly positioned disulfide bonds. Furthermore, occurrence of this wheat germ agglutinin-neurotoxin domain fold is predicted not only in the snake venom cardiotoxins and cytotoxins with neurotoxin-matched half-cystine sequence positions, but also for two small plant proteins, hevein and ragweed pollen allergen Ra5, on the basis of a nearly exact match of their half-cystine, sequence positions with those of the wheat germ agglutinin domain.

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Metadata

Authors
Drenth, J., Low, B. W., Richardson, J. S., & Wright, C. S.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1980-04
Volume
255
Issue
7
Pages
2652-2655
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1569916771
Cited by
158
References
0
FWCI
3.07
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core. https://app.cochat.ai/papers/10.1016/s0021-9258(19)85783-6
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Drenth, J., Low, B. W., Richardson, J. S., & Wright, C. S. (1980). The toxin-agglutinin fold. A new group of small protein structures organized around a four-disulfide core. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)85783-6

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.