The spider venoms often contain many active peptides such as neurotoxins,
lectins, inhibitors to enzyme, etc. These peptides are very important for
spider's hunting and defending. During the long history of spider evolution,
the peptides evolved into different structures and functions. Despite their
different biological functions the following peptides appear to have evolved
from the same ancestors and belong to the huwentoxin-1 family [1]:
Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena)
huwentoxin-I (HWTX-I), a 33 amino acid peptide, which can block the N-type
high-voltage activated calcium channels [2].
Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena)
huwentoxin-IV (HWTX-IV), a 35 amino acid peptide, which is an inhibitor of
tetrodotoxin (TTX) sensitive voltage-gated sodium channel [3].
Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena)
huwentoxin-V (HWTX-V), a 35 amino acid insecticidal toxin which can
reversibly paralyze in insects [4].
Ornithoctonus huwena (Chinese bird spider) (Selenocosmia huwena)
huwenlectin-I (SHL-I), a 32 amino acid peptide with haemagglutination
activity but almost no neurotoxin activity.
Brachypelma smithii (Mexican red knee tarantula) Venom protein 5.
Grammostola spatulata (Chilean rose tarantula) voltage sensor toxin 1.
Peptides of the huwentoxin type I family contain 6 cysteine residues involved
in three disulfide bonds. The three disulfide bridges have been assigned as
C1-C4, C2-C5 and C3-C6. HWTX-I adopts a compact structure consisting of a
small triple-stranded antiparallel β-sheet and five β-turns (see
<PDB:1QK6>) [6].
We developed a pattern for huwentoxin-1 family proteins, which have a
[C-C-CC-C-C] cysteine arrangement. The three-dimensional structure of
huwentoxin-1 family proteins possess a knottin scafold (see <PDOC60004>) [E1].
Isolation and characterization of hainantoxin-IV, a novel antagonist of tetrodotoxin-sensitive sodium channels from the Chinese bird spider Selenocosmia hainana.
Huwentoxin-V, a novel insecticidal peptide toxin from the spider Selenocosmia huwena, and a natural mutant of the toxin: indicates the key amino acid residues related to the biological activity.
Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana.
Proton nuclear magnetic resonance studies on huwentoxin-I from the venom of the spider Selenocosmia huwena: 2. Three-dimensional structure in solution.
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