1i25: Difference between revisions

Revision as of 14:07, 21 February 2008

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

Page seeded by OCA on Thu Feb 21 13:07:16 2008

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OCA

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-[[Image:1i25.jpg|left|200px]]<br /><applet load="1i25" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1i25.jpg|left|200px]]<br /><applet load="1i25" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1i25" />
 '''Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR'''<br />
 ==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.
+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==
-I25 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I25 OCA].
+I25 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==
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 [[Category: Ornithoctonus huwena]]
 [[Category: Single protein]]
-[[Category: Gu, X.C.]]
+[[Category: Gu, X C.]]
-[[Category: Liang, S.P.]]
+[[Category: Liang, S P.]]
-[[Category: Lu, S.Y.]]
+[[Category: Lu, S Y.]]
 [[Category: Shu, Q.]]
 [[Category: disulfide bonds]]
@@ Line 21: / Line 21: @@
 [[Category: neurotoxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:59:17 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:16 2008''