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Literature summary for 3.4.24.69 extracted from

  • Muraro, L.; Tosatto, S.; Motterlini, L.; Rossetto, O.; Montecucco, C.
    The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane (2009), Biochem. Biophys. Res. Commun., 380, 76-80.
    View publication on PubMed
Search for more literature for 3.4.24.69

Application

Application Comment Organism
medicine BoNT/A is largely employed in human therapy because of its specific inhibition of peripheral cholinergic nerve terminals Clostridium botulinum

Cloned(Commentary)

Cloned (Comment) Organism
expression of tagged heavy chain domain, as EGFP-Hc-N/A or mCherry-Hc-N/A, in Escherichia coli strain BL21(DE3) Clostridium botulinum

Localization

Localization Comment Organism GeneOntology No. Textmining
additional information the toxin binds to host plasma membrane of epithelial or neuronal cells, overview. Molecular modelling of Hc-N/A membrane binding via sphingomyelin-enriched membrane microdomains and phosphatidylinositol phosphates, overview Clostridium botulinum
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Clostridium botulinum BoNT/A binds to peripheral cholinergic nerve terminals, causing their inhibition, rapidly and with high specificity via its receptor binding, heavy chain domain termed HC. BoNT/A interacts specifically with polysialogangliosides and with a luminal loop of the synaptic vesicle protein SV2 via the C-terminal half of HC, while the N-terminal half of it binds to sphingomyelin-enriched membrane microdomains and shows defined interaction with phosphatidylinositol phosphates, that might play a role in the correct positioning of the toxin for the subsequent low pH-driven membrane insertion of translocation domain sHN. Molecular modelling of Hc-N/A membrane binding, overview ?
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Organism

Organism UniProt Comment Textmining
Clostridium botulinum
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information BoNT/A binds to peripheral cholinergic nerve terminals, causing their inhibition, rapidly and with high specificity via its receptor binding, heavy chain domain termed HC. BoNT/A interacts specifically with polysialogangliosides and with a luminal loop of the synaptic vesicle protein SV2 via the C-terminal half of HC, while the N-terminal half of it binds to sphingomyelin-enriched membrane microdomains and shows defined interaction with phosphatidylinositol phosphates, that might play a role in the correct positioning of the toxin for the subsequent low pH-driven membrane insertion of translocation domain sHN. Molecular modelling of Hc-N/A membrane binding, overview Clostridium botulinum ?
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Synonyms

Synonyms Comment Organism
BoNT/A
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 Clostridium botulinum
botulinum neurotoxin a
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 Clostridium botulinum