1i25: Difference between revisions

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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"
-caption="1i25" />
-'''Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR'''<br />
-==Overview==
+==Three dimensional solution structure of huwentoxin-II by 2D 1H-NMR==
-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.
+<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 ==
+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==
+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>
-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].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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]
+</div>
-[[Category: Ornithoctonus huwena]]
+<div class="pdbe-citations 1i25" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Gu, X.C.]]
+<references/>
-[[Category: Liang, S.P.]]
+__TOC__
-[[Category: Lu, S.Y.]]
+</StructureSection>
-[[Category: Shu, Q.]]
+[[Category: Cyriopagopus schmidti]]
-[[Category: disulfide bonds]]
+[[Category: Large Structures]]
-[[Category: insecticidal toxin]]
+[[Category: Gu XC]]
-[[Category: neurotoxin]]
+[[Category: Liang SP]]
+[[Category: Lu SY]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:59:17 2007''
+[[Category: Shu Q]]