Summary: Clostridium neurotoxin, C-terminal receptor binding
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Clostridium neurotoxin, C-terminal receptor binding Provide feedback
The Clostridium neurotoxin family is composed of tetanus neurotoxins and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (PF01742), the central translocation domains and two receptor binding domains . This domains is the C-terminal receptor binding domain, which adopts a modified beta-trefoil fold with a six stranded beta-barrel and a beta-hairpin triplet capping the domain . The first step in the intoxication process is a binding event between this domains and the pre-synaptic nerve ending .
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This tab holds annotation information from the InterPro database.
InterPro entry IPR013104
The Clostridium neurotoxin family is composed of tetanus neurotoxins and seven serotypes of botulinum neurotoxin. The structure of the botulinum neurotoxin reveals a four domain protein. The N-terminal catalytic domain (INTERPRO), the central translocation domains and two receptor-binding domains [PUBMED:9783750]. This domain is the C-terminal receptor-binding domain, which adopts a modified beta-trefoil fold with a six stranded beta-barrel and a beta-hairpin triplet capping the domain [PUBMED:9783750]. The first step in the intoxication process is a binding event between this domain and the pre-synaptic nerve ending [PUBMED:9783750].
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This family corresponds to a large set of related beta-trefoil proteins . The beta-trefoil is formed by six two-stranded hairpins . Three of these form a barrel structure and the other three are in a triangular array that caps the barrel. The arrangement of the secondary structures gives the molecules a pseudo 3-fold axis.
The clan contains the following 16 members:AbfB Agglutinin Botulinum_HA-17 CDtoxinA DUF569 Fascin FGF FRG1 IL1 Inhibitor_I66 Ins145_P3_rec Kunitz_legume MIR Ricin_B_lectin RicinB_lectin_2 Toxin_R_bind_C
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Curation and family details
|Seed source:||Pfam-B_3087 (release 15.0)|
|Number in seed:||2|
|Number in full:||159|
|Average length of the domain:||189.20 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||17.33 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||8|
|Download:||download the raw HMM for this family|
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There are 7 interactions for this family. More...
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Toxin_R_bind_C domain has been found. There are 88 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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