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1i25

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(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="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1i25" />
 
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'''Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR'''<br />
 
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==Overview==
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==Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR==
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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.
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<StructureSection load='1i25' size='340' side='right'caption='[[1i25]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1i25]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cyriopagopus_schmidti Cyriopagopus schmidti]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I25 FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i25 OCA], [https://pdbe.org/1i25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i25 RCSB], [https://www.ebi.ac.uk/pdbsum/1i25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i25 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TXH21_CYRSC TXH21_CYRSC] Lethal neurotoxin that blocks neuromuscular transmission. Acts cooperatively to potentiate the activity of huwentoxin-I. This toxin is active against insects.<ref>PMID:10424342</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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<ref>PMID:11790834</ref>
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I25 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11790834 11790834]
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</div>
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[[Category: Ornithoctonus huwena]]
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<div class="pdbe-citations 1i25" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Gu, X.C.]]
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<references/>
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[[Category: Liang, S.P.]]
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__TOC__
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[[Category: Lu, S.Y.]]
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</StructureSection>
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[[Category: Shu, Q.]]
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[[Category: Cyriopagopus schmidti]]
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[[Category: disulfide bonds]]
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[[Category: Large Structures]]
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[[Category: insecticidal toxin]]
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[[Category: Gu XC]]
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[[Category: neurotoxin]]
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[[Category: Liang SP]]
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[[Category: Lu SY]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:59:17 2007''
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[[Category: Shu Q]]

Current revision

Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR

PDB ID 1i25

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