Sandbox Reserved 966

This Sandbox is Reserved from 15/11/2014, through 15/05/2015 for use in the course "Biomolecule" taught by Bruno Kieffer at the Strasbourg University. This reservation includes Sandbox Reserved 951 through Sandbox Reserved 975.

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Structure of the "Clostridium botulinum" neurotoxin serotype A light chain with Zn2+ cofactor boundStructure of the "Clostridium botulinum" neurotoxin serotype A light chain with Zn2+ cofactor bound

<StructureSection load='3BON' size='340' side='right' caption='Caption for this structure' scene='60/604485/General_introduction/2'> The Clostridium botulinum neurotoxin produced by the bacteria Clostridium botulinum (and some strains of Clostridium butyricium and Clostridium baratii) is the most lethal toxin known today. Seven serotypically botulinum neurotoxins (BoNTs) have been found, each of them is categorized into subtypes depending on their amino acid sequence. The protein is initially synthesized as a single polypeptide chain of ≈150 kDa and is then cleaved by a protease to yield the mature toxin, which consists of a light chain (LC which is 50 kDa) and a heavy chain (HC which is 100 kDa). LC and HC are held together by a long peptide belt, non-covalent interactions and a single inter-chain disulphide bond The "Clostridium botulinum" neurotoxin serotype A light chain (BoNT/A-LC) shown below is composed of 425 residues. It was obtained with high resolution X-ray crystal structure using an inhibitory peptide and the catalytic Zn(II) ion.

StructureStructure

Global aspectGlobal aspect

BoNT/A-LC presents

File:Mecanisme3BON.jpg

Therapeutic applicationsTherapeutic applications

In the late 1960s, a Edward Schantz and a San Francisco opthalmologist, Alan Scott, start to work on the using of the botulinum toxine in therapeutic process. First, they try to treat strabismus and in the late 1970s the neurotoxine is used in many therapeutic applications.