1i25
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Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR
OverviewOverview
The three-dimensional structure of huwentoxin-II (HWTX-II), an, insecticidal peptide purified from the venom of spider Selenocosmia huwena, with a unique disulfide bond linkage as I-III, II-V, and IV-VI, has been, determined using 2D (1)H-NMR. The resulting structure of HWTX-II contains, two beta-turns (C4-S7 and K24-W27) and a double-stranded antiparallel, beta-sheet (W27-C29 and C34-K36). Although the C-terminal double-stranded, beta-sheet cross-linked by two disulfide bonds (II-V and IV-VI in HWTX-II, II-V and III-VI in the ICK molecules) is conserved both in HWTX-II and the, ICK molecules, the structure of HWTX-II is unexpected absence of the, cystine knot because of its unique disulfide linkage. It suggests that, HWTX-II adopts a novel scaffold different from the ICK motif that is, adopted by all other spider toxin structures elucidated thus far., Furthermore, the structure of HWTX-II, which conforms to the, disulfide-directed beta-hairpin (DDH) motif, not only supports the, hypothesis that the ICK is a minor elaboration of the more ancestral DDH, motif but also suggests that HWTX-II may have evolved from the same, structural ancestor.
About this StructureAbout this Structure
1I25 is a Single protein structure of sequence from Ornithoctonus huwena. Full crystallographic information is available from OCA.
ReferenceReference
The structure of spider toxin huwentoxin-II with unique disulfide linkage: evidence for structural evolution., Shu Q, Lu SY, Gu XC, Liang SP, Protein Sci. 2002 Feb;11(2):245-52. PMID:11790834
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