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 [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> | <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='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> | </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> | </table> | ||
== Function == | == Function == | ||
Latest revision as of 11:31, 6 November 2024
Three dimensional solution structure of huwentoxin-II by 2D 1H-NMRThree dimensional solution structure of huwentoxin-II by 2D 1H-NMR
Structural highlights
FunctionTXH21_CYRSC 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. References
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