| Autor: |
J.P. Robinson, J. Reidler |
| Rok vydání: |
1988 |
| Předmět: |
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| DOI: |
10.1016/s0076-6879(88)65055-5 |
| Popis: |
Publisher Summary This chapter describes the two-dimensional crystals of tetanus toxin. The mechanism by which toxin molecules traverse cell membranes remains unclear. This is because of both of the enzymatic nature of the active subunit and the difficulty of biochemical isolation of intermediates of proteins intimately associated with membranes. Three-dimensional (3D) crystals of some toxins are obtained but the mechanism of toxin entry is not yet elucidated. Although two-dimensional (2D) crystals are recently limited in resolution, the application of novel 2D crystallization techniques to toxins can provide further insight into the nature of the interactions between membranes and toxins. Tetanus toxin forms 2D crystals at monolayer surfaces analogous to the natural receptor and under conditions that mimic toxin entry. High-resolution toxin crystals formed at the membrane interface could provide a direct structural solution to the mechanism of toxin entry across the membrane. Preliminary observations of crystalline arrays of the structurally homologous botulinum toxin indicate a similar size and structure to the tetanus toxin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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