Structural Basis for Clostridial Neurotoxin Target Specificity

Name: Structural Basis for Clostridial Neurotoxin Target Specificity
Brand: VDM Verlag
SKU: 9783639104646
Price: 253.91 RON
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Autor: Mark Breidenbach

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Editura: VDM Verlag

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This thesis describes structural and biochemical§studies conducted on the most potent toxins known t...

Informații despre carte

Autor

Mark Breidenbach

Limbă

engleză

Legare

Carte - Carte broșată

Publicat

2008

Pagini

EAN

9783639104646

ISBN

3639104641

Enbook ID

06819439

Editura

VDM Verlag

Greutate

118

Dimensiuni

152 x 229 x 4

Descriere completă

This thesis describes structural and biochemical§studies conducted on the most potent toxins known to§man--clostridial neurotoxins. These remarkably§well-adapted proteins block neurotransmitter release§resulting in the paralytic conditions botulism and§tetanus. The toxins deliver highly specialized§proteases inside nerve cell where they act on§essential neuronal proteins called SNAREs with§unparalleled selectivity. Here, x-ray crystallography§is employed to obtain a high-resolution structure of§a botulinum neurotoxin protease in complex with its§target SNARE. The determinants of the protease's§exquisite specificity are shown to be an array of§previously unknown binding sites that enhance§catalytic efficiency. Additionally, structural§studies of tetanus neurotoxin were conducted and are§described within. The function of clostridial§neurotoxins is beautifully reflected in their§architecture; the molecular structures described here§reveal how these amazing proteins seek and destroy§their intracellular targets. Ultimately, this§research could be applied to the development of novel§and extremely specific inhibitors of these§extraordinarily powerful neurotoxins. This thesis describes structural and biochemical§studies conducted on the most potent toxins known to§man--clostridial neurotoxins. These remarkably§well-adapted proteins block neurotransmitter release§resulting in the paralytic conditions botulism andtetanus. The toxins deliver highly specialized§proteases inside nerve cell where they act on§essential neuronal proteins called SNAREs with§unparalleled selectivity. Here, x-ray crystallography§is employed to obtain a high-resolution structure of§a botulinum neurotoxin protease in complex with its§target SNARE. The determinants of the protease''s§exquisite specificity are shown to be an array of§previously unknown binding sites that enhance§catalytic efficiency. Additionally, structural§studies of tetanus neurotoxin were conducted and are§described within. The function of clostridial§neurotoxins is beautifully reflected in their§architecture; the molecular structures described here§reveal how these amazing proteins seek and destroy§their intracellular targets. Ultimately, this§research could be applied to the development of novel§and extremely specific inhibitors of these§extraordinarily powerful neurotoxins.

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Structural Basis for Clostridial Neurotoxin Target Specificity

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