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1i25
From Proteopedia
(New page: 200px<br /><applet load="1i25" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i25" /> '''Three dimensional solution structure of huwe...) |
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| - | [[Image:1i25.jpg|left|200px]]<br /><applet load="1i25" size=" | + | [[Image:1i25.jpg|left|200px]]<br /><applet load="1i25" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i25" /> | caption="1i25" /> | ||
'''Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR'''<br /> | '''Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of huwentoxin-II (HWTX-II), an | + | 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 Structure== | ==About this Structure== | ||
| - | 1I25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ornithoctonus_huwena Ornithoctonus huwena]. Full crystallographic information is available from [http:// | + | 1I25 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ornithoctonus_huwena Ornithoctonus huwena]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I25 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ornithoctonus huwena]] | [[Category: Ornithoctonus huwena]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gu, X | + | [[Category: Gu, X C.]] |
| - | [[Category: Liang, S | + | [[Category: Liang, S P.]] |
| - | [[Category: Lu, S | + | [[Category: Lu, S Y.]] |
[[Category: Shu, Q.]] | [[Category: Shu, Q.]] | ||
[[Category: disulfide bonds]] | [[Category: disulfide bonds]] | ||
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[[Category: neurotoxin]] | [[Category: neurotoxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:16 2008'' |
Revision as of 11:07, 21 February 2008
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Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR
Overview
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 Structure
1I25 is a Single protein structure of sequence from Ornithoctonus huwena. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:07:16 2008
