Sandbox Reserved 466
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The ''Clostridium tetani'' precursor polypeptide is cleaved during cell autolysis into a heavy and light chains. These two chains remain linked by a disulfide bridge. These chains are non-toxic when separated. | The ''Clostridium tetani'' precursor polypeptide is cleaved during cell autolysis into a heavy and light chains. These two chains remain linked by a disulfide bridge. These chains are non-toxic when separated. | ||
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Revision as of 14:15, 1 May 2012
Contents |
TETANUS TOXIN
This Sandbox is Reserved from 13/03/2012, through 01/06/2012 for use in the course "Proteins and Molecular Mechanisms" taught by Robert B. Rose at the North Carolina State University, Raleigh, NC USA. This reservation includes Sandbox Reserved 451 through Sandbox Reserved 500. | ||||||
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More help: Help:Editing For more help, look at this link: http://www.proteopedia.org/wiki/index.php/Help:Getting_Started_in_Proteopedia IntroductionThe tetanus toxin, or Clostridium tetani, is produced by the bacteria Clostridium. Clostridium bacteria produces distinct neurotoxins that are extremely potent to humans. It releases two types of neurotoxins: Clostridium botulinum and Clostridium tetani. It is part of the peptidase M27 family of proteins, which are metalloproteases. Metalloproteases bind with a divalent cation, usually zinc, which activates water molecules within the active site to hydrolyze peptide bonds. Clostridium tetani functions by inhibiting neurotransmitter release into the synaptic cleft of the spinal cord. It mimics a zinc peptidase The toxin is produced after the bacterial cell's active, exponential growth phase.
Structure
The Clostridium tetani precursor polypeptide is cleaved during cell autolysis into a heavy and light chains. These two chains remain linked by a disulfide bridge. These chains are non-toxic when separated. The heavy chain is involved in binding and the light chain is involved in biological activity.
Mechanism of ActionMedical Implications or Possible Applications |