Irditoxin

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disulfide bonds are shown as yellow sticks. The intramolecular disulfide bond at the dimer interface is shown as green and yellow spheres.[1]
Irditoxin subunit A
Identifiers
OrganismBoiga irregularis
Symbol3NBA
UniProt
A0S864
Search for
StructuresSwiss-model
DomainsInterPro
Irdixotin subunit B
Identifiers
OrganismBoiga irregularis
Symbol3NBB
UniProt
A0S865
Search for
StructuresSwiss-model
DomainsInterPro

Irditoxin is a

disulfide bond. This structure is unusual for 3FTx proteins, which are most commonly monomeric.[1][2][3]

Structure

amino acid residues long, respectively, and each possess a seven-residue extension with a pyroglutamic acid post-translational modification at the N-terminus.[1][2]

Irditoxin's structure is highly unusual within the 3FTx superfamily.

protein-protein interaction surface;[2] the recently described alpha-cobratoxin also forms both covalent homodimers and low-abundance covalent heterodimers with other 3FTx proteins found in monocled cobra (Naja kaouthia) venom.[4] It is as yet unclear how irditoxin's two subunits contribute to its biological activities.[2]

Function

Irditoxin is an abundant protein in the venom of the brown tree snake and accounts for about 10% of the protein found in venom samples of brown treesnakes collected from Guam, where they are an invasive species. Irditoxin's toxic effects are highly species-dependent; in laboratory tests, it is highly toxic to lizards and birds but not to mammals. Although the molecular mechanism of toxicity is not clear, irditoxin produces robust post-synaptic blockade of signaling in the avian neuromuscular junction.[1]

Discovery and nomenclature

Irditoxin was first described in 2009 after isolation from samples of venom from the

colubrid snakes, likely possess homologous proteins.[5]
: 18 

References

  1. ^
    S2CID 4816592
    .
  2. ^
    PMID 20670641
    .
  3. S2CID 6377409
    .
  4. PMID 22223648
    .
  5. OCLC 757355711
    .
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