1nix
From Proteopedia
(New page: 200px<br /><applet load="1nix" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nix" /> '''THREE DIMENSIONAL SOLUTION STRUCTURE OF HAIN...) |
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'''THREE DIMENSIONAL SOLUTION STRUCTURE OF HAINANTOXIN-I BY 2D 1H-NMR'''<br /> | '''THREE DIMENSIONAL SOLUTION STRUCTURE OF HAINANTOXIN-I BY 2D 1H-NMR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hainantoxin-I is a novel peptide toxin, purified from the venom of the | + | Hainantoxin-I is a novel peptide toxin, purified from the venom of the Chinese bird spider Selenocosmia hainana (=Ornithoctonus hainana). It includes 33 amino acid residues with a disulfide linkage of I-IV, II-V and III-VI, assigned by partial reduction and sequence analysis. Under two-electrode voltage-clamp conditions, hainantoxin-I can block rNa(v)1.2/beta(1) and the insect sodium channel para/tipE expressed in Xenopus laevis oocytes with IC(50) values of 68+/-6 microM and 4.3+/-0.3 microM respectively. The three-dimensional solution structure of hainantoxin-I belongs to the inhibitor cystine knot structural family determined by two-dimensional (1)H nuclear magnetic resonance techniques. Structural comparison of hainantoxin-I with those of other toxins suggests that the combination of the charged residues and a vicinal hydrophobic patch should be responsible for ligand binding. This is the first report of an insect sodium channel blocker from spider venom and it provides useful information for the structure-function relationship studies of insect sodium channels. |
==About this Structure== | ==About this Structure== | ||
| - | 1NIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ornithoctonus_hainana Ornithoctonus hainana] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1NIX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ornithoctonus_hainana Ornithoctonus hainana] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIX OCA]. |
==Reference== | ==Reference== | ||
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[[Category: inhibitor cystine knot motif]] | [[Category: inhibitor cystine knot motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:45 2008'' |
Revision as of 12:06, 21 February 2008
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THREE DIMENSIONAL SOLUTION STRUCTURE OF HAINANTOXIN-I BY 2D 1H-NMR
Overview
Hainantoxin-I is a novel peptide toxin, purified from the venom of the Chinese bird spider Selenocosmia hainana (=Ornithoctonus hainana). It includes 33 amino acid residues with a disulfide linkage of I-IV, II-V and III-VI, assigned by partial reduction and sequence analysis. Under two-electrode voltage-clamp conditions, hainantoxin-I can block rNa(v)1.2/beta(1) and the insect sodium channel para/tipE expressed in Xenopus laevis oocytes with IC(50) values of 68+/-6 microM and 4.3+/-0.3 microM respectively. The three-dimensional solution structure of hainantoxin-I belongs to the inhibitor cystine knot structural family determined by two-dimensional (1)H nuclear magnetic resonance techniques. Structural comparison of hainantoxin-I with those of other toxins suggests that the combination of the charged residues and a vicinal hydrophobic patch should be responsible for ligand binding. This is the first report of an insect sodium channel blocker from spider venom and it provides useful information for the structure-function relationship studies of insect sodium channels.
About this Structure
1NIX is a Single protein structure of sequence from Ornithoctonus hainana with as ligand. Full crystallographic information is available from OCA.
Reference
Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana., Li D, Xiao Y, Hu W, Xie J, Bosmans F, Tytgat J, Liang S, FEBS Lett. 2003 Dec 18;555(3):616-22. PMID:14675784
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