IPR012928
Clostridium neurotoxin, receptor binding N-terminal
InterPro entry
Short name | Toxin_rcpt-bd_N |
Overlapping homologous superfamilies |
Description
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
Cross References
Contributing Member Database Entry
- Pfam:PF07953