1kqi
From Proteopedia
(New page: 200px<br /><applet load="1kqi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kqi" /> '''NMR Solution Structure of the trans Pro30 Is...) |
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'''NMR Solution Structure of the trans Pro30 Isomer of ACTX-Hi:OB4219'''<br /> | '''NMR Solution Structure of the trans Pro30 Isomer of ACTX-Hi:OB4219'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The primary sequence and three-dimensional structure of a novel peptide | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1KQI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hadronyche_infensa Hadronyche infensa]. Full crystallographic information is available from [http:// | + | 1KQI is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hadronyche_infensa Hadronyche infensa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hadronyche infensa]] | [[Category: Hadronyche infensa]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Alewood, P | + | [[Category: Alewood, P F.]] |
| - | [[Category: Craik, D | + | [[Category: Craik, D J.]] |
| - | [[Category: Daly, N | + | [[Category: Daly, N L.]] |
| - | [[Category: Rosengren, K | + | [[Category: Rosengren, K J.]] |
[[Category: Wilson, D.]] | [[Category: Wilson, D.]] | ||
[[Category: cis-trans isomerisation]] | [[Category: cis-trans isomerisation]] | ||
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[[Category: spider venom]] | [[Category: spider venom]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:54 2008'' |
Revision as of 11:36, 21 February 2008
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NMR Solution Structure of the trans Pro30 Isomer of ACTX-Hi:OB4219
Overview
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.
About this Structure
1KQI is a Protein complex structure of sequences from Hadronyche infensa. Full crystallographic information is available from OCA.
Reference
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
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