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1vtx

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{{STRUCTURE_1vtx| PDB=1vtx | SCENE= }}
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'''DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, 20 STRUCTURES'''
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===DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, 20 STRUCTURES===
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==Overview==
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BACKGROUND: Versutoxin (delta-ACTX-Hv1) is the major component of the venom of the Australian Blue Mountains funnel web spider, Hadronyche versuta. delta-ACTX-Hv1 produces potentially fatal neurotoxic symptoms in primates by slowing the inactivation of voltage-gated sodium channels; delta-ACTX-Hv1 is therefore a useful tool for studying sodium channel function. We have determined the three-dimensional structure of delta-ACTX-Hv1 as the first step towards understanding the molecular basis of its interaction with these channels. RESULTS: The solution structure of delta-ACTX-Hv1, determined using NMR spectroscopy, comprises a core beta region containing a triple-stranded antiparallel beta sheet, a thumb-like extension protruding from the beta region and a C-terminal 310 helix that is appended to the beta domain by virtue of a disulphide bond. The beta region contains a cystine knot motif similar to that seen in other neurotoxic polypeptides. The structure shows homology with mu-agatoxin-I, a spider toxin that also modifies the inactivation kinetics of vertebrate voltage-gated sodium channels. More surprisingly, delta-ACTX-Hv1 shows both sequence and structural homology with gurmarin, a plant polypeptide. This similarity leads us to suggest that the sweet-taste suppression elicited by gurmarin may result from an interaction with one of the downstream ion channels involved in sweet-taste transduction. CONCLUSIONS: delta-ACTX-Hv1 shows no structural homology with either sea anemone or alpha-scorpion toxins, both of which also modify the inactivation kinetics of voltage-gated sodium channels by interacting with channel recognition site 3. However, we have shown that delta-ACTX-Hv1 contains charged residues that are topologically related to those implicated in the binding of sea anemone and alpha-scorpion toxins to mammalian voltage-gated sodium channels, suggesting similarities in their mode of interaction with these channels.
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{{ABSTRACT_PUBMED_9384567}}
==About this Structure==
==About this Structure==
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1VTX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hadronyche_versuta Hadronyche versuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VTX OCA].
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1VTX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hadronyche_versuta Hadronyche versuta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VTX OCA].
==Reference==
==Reference==
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[[Category: Sodium channel toxin]]
[[Category: Sodium channel toxin]]
[[Category: Venom]]
[[Category: Venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:03:37 2008''

Revision as of 09:03, 29 July 2008

Image:1vtx.png

Template:STRUCTURE 1vtx

DELTA-ATRACOTOXIN-HV1 (VERSUTOXIN) FROM HADRONYCHE VERSUTA, NMR, 20 STRUCTURES

Template:ABSTRACT PUBMED 9384567

About this Structure

1VTX is a Single protein structure of sequence from Hadronyche versuta. Full experimental information is available from OCA.

Reference

The structure of versutoxin (delta-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel., Fletcher JI, Chapman BE, Mackay JP, Howden ME, King GF, Structure. 1997 Nov 15;5(11):1525-35. PMID:9384567

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