1i25
From Proteopedia
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| - | [[Image:1i25.jpg|left|200px]] | ||
| - | + | ==Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR== | |
| - | + | <StructureSection load='1i25' size='340' side='right'caption='[[1i25]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <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> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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> |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [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> | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == 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. | 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 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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| - | The structure of spider toxin huwentoxin-II with unique disulfide linkage: evidence for structural evolution., Shu Q, Lu SY, Gu XC, Liang SP | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 1i25" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cyriopagopus schmidti]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gu XC]] | ||
| + | [[Category: Liang SP]] | ||
| + | [[Category: Lu SY]] | ||
| + | [[Category: Shu Q]] | ||
Current revision
Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR
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