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Details on Person BoNTs are synthesized as polypeptides of 150 kDa that are cl...
| Class:Id | Summation:181688 |
|---|---|
| _displayName | BoNTs are synthesized as polypeptides of 150 kDa that are cl... |
| _timestamp | 2007-08-02 18:48:21 |
| created | [InstanceEdit:181679] Gopinathrao, G, 2006-06-15 22:12:23 |
| modified | [InstanceEdit:190033] Gopinathrao, G, 2006-12-13 17:03:37 [InstanceEdit:194803] Gopinathrao, G, 2007-03-27 17:24:22 [InstanceEdit:194822] Gopinathrao, G, 2007-03-28 15:45:04 [InstanceEdit:195119] D'Eustachio, P, 2007-04-02 19:50:31 [InstanceEdit:201255] Gopinathrao, G, 2007-08-02 18:49:02 |
| text | BoNTs are synthesized as polypeptides of 150 kDa that are cleaved into heavy and light chains linked by a single disulfide bond. Cleavage takes place within a surface-exposed loop at the N-terminal of the Heavy chain subunit. Both bacterial and host endopeptidases can catalyze BoNT cleavage into heavy and light chains, but host enzymes are thought to carry out this function in vivo. The Heavy Chain (HC) has two 50 kDa functional domains: the N-terminal translocation domain is capable of forming channels in lipid bilayers; the C-terminal ganglioside-binding domain is important for membrane binding and subsequent internalization of toxins by host neurons. The 50 kDa Light chain (LC) is a zinc-dependent endopeptidase specific for core components of neurotransmitter release complexes. |
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No pathways have been reviewed or authored by BoNTs are synthesized as polypeptides of 150 kDa that are cl... (181688)
