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| | ==NMR Solution Structure of the trans Pro30 Isomer of ACTX-Hi:OB4219== | | ==NMR Solution Structure of the trans Pro30 Isomer of ACTX-Hi:OB4219== |
| - | <StructureSection load='1kqi' size='340' side='right' caption='[[1kqi]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1kqi' size='340' side='right'caption='[[1kqi]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kqi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hadronyche_infensa Hadronyche infensa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KQI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hadronyche_infensa Hadronyche infensa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KQI FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kqh|1kqh]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1kqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kqi RCSB], [http://www.ebi.ac.uk/pdbsum/1kqi PDBsum]</span></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=1kqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kqi OCA], [https://pdbe.org/1kqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kqi RCSB], [https://www.ebi.ac.uk/pdbsum/1kqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kqi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/T21A_HADIN T21A_HADIN] Inhibits sodium channels (Nav) of insects. |
| | <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 1kqi" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Hadronyche infensa]] | | [[Category: Hadronyche infensa]] |
| - | [[Category: Alewood, P F]] | + | [[Category: Large Structures]] |
| - | [[Category: Craik, D J]] | + | [[Category: Alewood PF]] |
| - | [[Category: Daly, N L]] | + | [[Category: Craik DJ]] |
| - | [[Category: Rosengren, K J]] | + | [[Category: Daly NL]] |
| - | [[Category: Wilson, D]] | + | [[Category: Rosengren KJ]] |
| - | [[Category: Cis-trans isomerisation]] | + | [[Category: Wilson D]] |
| - | [[Category: Cystine knot]]
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| - | [[Category: Disulfide rich]]
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| - | [[Category: Funnel web]]
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| - | [[Category: Nmr spectroscopy]]
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| - | [[Category: Solution structure]]
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| - | [[Category: Spider venom]]
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| - | [[Category: Toxin]]
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| Structural highlights
Function
T21A_HADIN Inhibits sodium channels (Nav) of insects.
Publication Abstract from PubMed
The primary sequence and three-dimensional structure of a novel peptide toxin isolated from the Australian funnel-web spider Hadronyche infensa sp. is reported. ACTX-Hi:OB4219 contains 38 amino acids, including eight-cysteine residues that form four disulfide bonds. The connectivities of these disulfide bonds were previously unknown but have been unambiguously determined in this study. Three of these disulfide bonds are arranged in an inhibitor cystine-knot (ICK) motif, which is observed in a range of other disulfide-rich peptide toxins. The motif incorporates an embedded ring in the structure formed by two of the disulfides and their connecting backbone segments penetrated by a third disulfide bond. Using NMR spectroscopy, we determined that despite the isolation of a single native homologous product by RP-HPLC, ACTX-Hi:OB4219 possesses two equally populated conformers in solution. These two conformers were determined to arise from cis/trans isomerization of the bond preceding Pro30. Full assignment of the NMR spectra for both conformers allowed for the calculation of their structures, revealing the presence of a triple-stranded antiparallel beta sheet consistent with the inhibitor cystine-knot (ICK) motif.
Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche Infensa sp. that contains a cystine-knot motif within its four disulfide bonds.,Rosengren KJ, Wilson D, Daly NL, Alewood PF, Craik DJ Biochemistry. 2002 Mar 12;41(10):3294-301. PMID:11876637[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rosengren KJ, Wilson D, Daly NL, Alewood PF, Craik DJ. Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche Infensa sp. that contains a cystine-knot motif within its four disulfide bonds. Biochemistry. 2002 Mar 12;41(10):3294-301. PMID:11876637
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