2axk

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

2axk is a 1 chain structure with sequence from Tityus discrepans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 10 models
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Solution structure of discrepin, a scorpion venom toxin blocking K+ channels.==
-<StructureSection load='2axk' size='340' side='right'caption='[[2axk]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='2axk' size='340' side='right'caption='[[2axk]]' scene=''>
 == Structural highlights ==
-<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 [https://proteopedia.org/fgij/fg.htm?mol=2AXK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2axk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tityus_discrepans Tityus discrepans]. 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 [https://proteopedia.org/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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=2axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2axk OCA], [https://pdbe.org/2axk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2axk RCSB], [https://www.ebi.ac.uk/pdbsum/2axk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2axk ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KA156_TITDI KA156_TITDI]] Irreversibly blocks the A-type voltage-gated potassium channels in rat cerebellum granular cells.<ref>PMID:15369825</ref> <ref>PMID:16460026</ref>
+[https://www.uniprot.org/uniprot/KA156_TITDI KA156_TITDI] Irreversibly blocks the A-type voltage-gated potassium channels in rat cerebellum granular cells.<ref>PMID:15369825</ref> <ref>PMID:16460026</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Corzo, G]]
+[[Category: Tityus discrepans]]
-[[Category: Delepierre, M]]
+[[Category: Corzo G]]
-[[Category: Martin-Eauclaire, M F]]
+[[Category: D'Suze G]]
-[[Category: Murgia, A R]]
+[[Category: Delepierre M]]
-[[Category: Possani, L D]]
+[[Category: Martin-Eauclaire M-F]]
-[[Category: Prestipino, G]]
+[[Category: Murgia AR]]
-[[Category: Prochnicka-Chalufour, A]]
+[[Category: Possani LD]]
-[[Category: Satake, H]]
+[[Category: Prestipino G]]
-[[Category: Suze, G D]]
+[[Category: Prochnicka-Chalufour A]]
-[[Category: A-current]]
+[[Category: Satake H]]
-[[Category: Discrepin]]
-[[Category: K+-channel]]
-[[Category: Scorpion toxin]]
-[[Category: Toxin]]

2axk

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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