Solution structure of omega-agatoxin-Aa4a from Agelenopsis aperta.[1]
Identifiers
Symbol
Toxin_9
Pfam
PF02819
Pfam clan
CL0083
InterPro
IPR004169
SCOP2
1oav / SCOPe / SUPFAM
OPM superfamily
112
OPM protein
1agg
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Delta Atracotoxin
Identifiers
Symbol
Atracotoxin
Pfam
PF05353
InterPro
IPR008017
SCOP2
1qdp / SCOPe / SUPFAM
OPM protein
1vtx
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Spider toxin CSTX family
Identifiers
Symbol
Toxin_35
Pfam
PF10530
InterPro
IPR011142
PROSITE
PDOC60029
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Spider potassium channel inhibitory toxin
Identifiers
Symbol
Toxin_12
Pfam
PF07740
Pfam clan
CL0083
InterPro
IPR011696
SCOP2
1d1h / SCOPe / SUPFAM
OPM superfamily
112
OPM protein
1qk6
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Spider toxins are a family of proteins produced by spiders which function as neurotoxins. The mechanism of many spider toxins is through blockage of calcium channels.
A remotely related group of atracotoxins operate by opening sodium channels. Delta atracotoxin from the venom of the Sydney funnel-web spider produces potentially fatal neurotoxic symptoms in primates by slowing the inactivation of voltage-gated sodium channels.[2] The structure of atracotoxin comprises a core beta region containing a triple-stranded a thumb-like extension protruding from the beta region and a C-terminal helix. The beta region contains a cystine knot motif, a feature seen in other neurotoxic polypeptides[2] and other spider toxins, of the CSTX family.
Spider potassium channel inhibitory toxins is another group of spider toxins. A representative of this group is hanatoxin, a 35 amino acid peptide toxin which was isolated from Chilean rose tarantula (Grammostola rosea, syn. G. spatulata) venom. It inhibits the drk1 voltage-gated potassium channel by altering the energetics of gating.[3] See also Huwentoxin-1.[4]
^ abMackay JP, King GF, Fletcher JI, Chapman BE, Howden ME (1997). "The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel". Structure. 5 (11): 1525–1535. doi:10.1016/S0969-2126(97)00301-8. PMID 9384567.
^Shimada I, Sato K, Takahashi H, Kim JI, Min HJ, Swartz KJ (2000). "Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins". J. Mol. Biol. 297 (3): 771–780. doi:10.1006/jmbi.2000.3609. PMID 10731427.
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Tetanus toxin (TeNT) is an extremely potent neurotoxin produced by the vegetative cell of Clostridium tetani in anaerobic conditions, causing tetanus...
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