D
IPR012928

Clostridium neurotoxin, receptor binding N-terminal

InterPro entry
Short nameToxin_rcpt-bd_N
Overlapping
homologous
superfamilies
 

Description

The Clostridium neurotoxin family is composed of tetanus neurotoxin and seven serotypes of botulinum neurotoxin. These toxins act as inhibitors of neurotransmitter release
[2, 3]
.

The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (
IPR000395
), the central translocation domain and two receptor binding domains
[1]
. This domain is the N-terminal receptor binding domain, which is comprised of two seven-stranded β-sheets sandwiched together to form a jelly role motif
[1]
. The role of this domain in receptor binding appears to be indirect.

References

1.Crystal structure of botulinum neurotoxin type A and implications for toxicity. Lacy DB, Tepp W, Cohen AC, DasGupta BR, Stevens RC. Nat. Struct. Biol. 5, 898-902, (1998). View articlePMID: 9783750

2.Tetanus toxin inhibits depolarization-stimulated protein phosphorylation in rat cortical synaptosomes: effect on synapsin I phosphorylation and translocation. Presek P, Jessen S, Dreyer F, Jarvie PE, Findik D, Dunkley PR. J. Neurochem. 59, 1336-43, (1992). View articlePMID: 1328520

3.Botulinum toxins: mechanisms of action, antinociception and clinical applications. Wheeler A, Smith HS. Toxicology 306, 124-46, (2013). View articlePMID: 23435179

GO terms

biological process

  • None

molecular function

  • None

Cross References

Contributing Member Database Entry
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.