2axk: Difference between revisions

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[[Image:2axk.gif|left|200px]]
{{Seed}}
[[Image:2axk.png|left|200px]]


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{{STRUCTURE_2axk|  PDB=2axk  |  SCENE=  }}  
{{STRUCTURE_2axk|  PDB=2axk  |  SCENE=  }}  


'''Solution structure of discrepin, a scorpion venom toxin blocking K+ channels.'''
===Solution structure of discrepin, a scorpion venom toxin blocking K+ channels.===




==Overview==
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Discrepin, isolated from the venom of the Venezuelan scorpion Tityus discrepans, blocks preferentially the I(A) currents of the voltage-dependent K+ channel of rat cerebellum granular cells in an irreversible way. It contains 38 amino acid residues with a pyroglutamic acid as the N-terminal residue [D'Suze, G., Batista, C. V., Frau, A., Murgia, A. R., Zamudio, F. Z., Sevcik, C., Possani, L. D., and Prestipino, G. (2004) Arch. Biochem. Biophys. 430, 256-63]. It is the most distinctive member of the alpha-KTx15 subfamily of scorpion toxins. Six members of the alpha-KTx15 subfamily have been reported so far to be specific for this subtype of the K+ channel; however, none of them have had their three-dimensional structure determined, and no information for the residues possibly involved in channel recognition and binding is available. Natural discrepin (n-discrepin) was prepared from scorpion venom, and its synthetic analogue (s-discrepin) was obtained by solid-phase synthesis. Analysis of two-dimensional 1H NMR spectra of n- and s-discrepin indicates that both peptides have the same structure. Here we report the solution structure of s-discrepin determined by NMR using 565 meaningful distance constraints derived from the volume integration of the two-dimensional NOESY spectrum, 22 dihedrals, and three hydrogen bonds. Discrepin displays the alpha/beta scaffold, characteristic of scorpion toxins. Some features of the proposed interacting surface between the toxin and channel as well as the opposite "alpha-helix surface" are discussed in comparison with those of other alpha-KTx15 members. Both n- and s-discrepin exhibit similar physiological actions as verified by patch-clamp and binding and displacement experiments.
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{{ABSTRACT_PUBMED_16460026}}


==About this Structure==
==About this Structure==
2AXK is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXK OCA].  
2AXK is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXK OCA].  


==Reference==
==Reference==
Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily., Prochnicka-Chalufour A, Corzo G, Satake H, Martin-Eauclaire MF, Murgia AR, Prestipino G, D'Suze G, Possani LD, Delepierre M, Biochemistry. 2006 Feb 14;45(6):1795-804. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460026 16460026]
Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily., Prochnicka-Chalufour A, Corzo G, Satake H, Martin-Eauclaire MF, Murgia AR, Prestipino G, D'Suze G, Possani LD, Delepierre M, Biochemistry. 2006 Feb 14;45(6):1795-804. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460026 16460026]
Discrepin, a new peptide of the sub-family alpha-ktx15, isolated from the scorpion Tityus discrepans irreversibly blocks K+ -channels (IA currents) of cerebellum granular cells., D'Suze G, Batista CV, Frau A, Murgia AR, Zamudio FZ, Sevcik C, Possani LD, Prestipino G, Arch Biochem Biophys. 2004 Oct 15;430(2):256-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15369825 15369825]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Corzo, G.]]
[[Category: Corzo, G.]]
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[[Category: Nmr]]
[[Category: Nmr]]
[[Category: Scorpion toxin]]
[[Category: Scorpion toxin]]
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