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| - | [[Image:2axk.gif|left|200px]] | |
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| - | <!-- | + | ==Solution structure of discrepin, a scorpion venom toxin blocking K+ channels.== |
| - | The line below this paragraph, containing "STRUCTURE_2axk", creates the "Structure Box" on the page.
| + | <StructureSection load='2axk' size='340' side='right'caption='[[2axk]]' scene=''> |
| - | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
| - | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <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> |
| - | or leave the SCENE parameter empty for the default display.
| + | </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> |
| - | {{STRUCTURE_2axk| PDB=2axk | SCENE= }}
| + | <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> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == 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. |
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| - | '''Solution structure of discrepin, a scorpion venom toxin blocking K+ channels.'''
| + | 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<ref>PMID:16460026</ref> |
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| - | ==Overview==
| + | |
| - | 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.
| + | |
| | | | |
| - | ==About this Structure==
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | 2AXK is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AXK OCA].
| + | </div> |
| | + | <div class="pdbe-citations 2axk" style="background-color:#fffaf0;"></div> |
| | | | |
| - | ==Reference== | + | ==See Also== |
| - | 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]
| + | *[[Potassium channel toxin 3D structures|Potassium channel toxin 3D structures]] |
| - | [[Category: Single protein]] | + | == References == |
| - | [[Category: Corzo, G.]] | + | <references/> |
| - | [[Category: Delepierre, M.]] | + | __TOC__ |
| - | [[Category: Martin-Eauclaire, M F.]] | + | </StructureSection> |
| - | [[Category: Murgia, A R.]] | + | [[Category: Large Structures]] |
| - | [[Category: Possani, L D.]] | + | [[Category: Tityus discrepans]] |
| - | [[Category: Prestipino, G.]] | + | [[Category: Corzo G]] |
| - | [[Category: Prochnicka-Chalufour, A.]] | + | [[Category: D'Suze G]] |
| - | [[Category: Satake, H.]] | + | [[Category: Delepierre M]] |
| - | [[Category: Suze, G D.]]
| + | [[Category: Martin-Eauclaire M-F]] |
| - | [[Category: A-current]]
| + | [[Category: Murgia AR]] |
| - | [[Category: Discrepin]]
| + | [[Category: Possani LD]] |
| - | [[Category: K+-channel]]
| + | [[Category: Prestipino G]] |
| - | [[Category: Nmr]]
| + | [[Category: Prochnicka-Chalufour A]] |
| - | [[Category: Scorpion toxin]]
| + | [[Category: Satake H]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:35:50 2008''
| + | |
| Structural highlights
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.
See Also
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
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