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2axk

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Revision as of 21:10, 9 September 2015

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

Structural highlights

2axk is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[KA156_TITDI] Irreversibly blocks the A-type voltage-gated potassium channels in rat cerebellum granular cells.^[1] ^[2]

Publication Abstract from PubMed

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.

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:16460026^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ D'Suze G, Batista CV, Frau A, Murgia AR, Zamudio FZ, Sevcik C, Possani LD, Prestipino G. 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. Arch Biochem Biophys. 2004 Oct 15;430(2):256-63. PMID:15369825 doi:10.1016/j.abb.2004.07.010
↑ Prochnicka-Chalufour A, Corzo G, Satake H, Martin-Eauclaire MF, Murgia AR, Prestipino G, D'Suze G, Possani LD, Delepierre M. Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily. Biochemistry. 2006 Feb 14;45(6):1795-804. PMID:16460026 doi:10.1021/bi0519248
↑ Prochnicka-Chalufour A, Corzo G, Satake H, Martin-Eauclaire MF, Murgia AR, Prestipino G, D'Suze G, Possani LD, Delepierre M. Solution structure of discrepin, a new K+-channel blocking peptide from the alpha-KTx15 subfamily. Biochemistry. 2006 Feb 14;45(6):1795-804. PMID:16460026 doi:10.1021/bi0519248

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2axk"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[2axk]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AXK FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=2axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2axk RCSB], [http://www.ebi.ac.uk/pdbsum/2axk PDBsum]</span></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=2axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axk OCA], [http://pdbe.org/2axk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2axk RCSB], [http://www.ebi.ac.uk/pdbsum/2axk PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2axk" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2axk

From Proteopedia

Revision as of 21:10, 9 September 2015

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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