1i25: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1i25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haplopelma_schmidti Haplopelma 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I25 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1i25]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Haplopelma_schmidti Haplopelma 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I25 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i25 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i25 RCSB], [http://www.ebi.ac.uk/pdbsum/1i25 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i25 OCA], [http://pdbe.org/1i25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i25 RCSB], [http://www.ebi.ac.uk/pdbsum/1i25 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://www.uniprot.org/uniprot/TXH21_HAPSC TXH21_HAPSC]] 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1i25" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 04:42, 12 September 2015
Three dimensional solution structure of huwentoxin-II by 2D 1H-NMRThree dimensional solution structure of huwentoxin-II by 2D 1H-NMR
Structural highlights
Function[TXH21_HAPSC] Lethal neurotoxin that blocks neuromuscular transmission. Acts cooperatively to potentiate the activity of huwentoxin-I. This toxin is active against insects.[1] Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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