1kcp

From Proteopedia

(Difference between revisions)

Revision as of 07:22, 18 May 2023

3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES

Structural highlights

1kcp is a 1 chain structure with sequence from Conus purpurascens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

O17A_CONPU Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the drosophila Shaker channel (IC(50)=57-80 nM) (PubMed:12074021, PubMed:10818087, PubMed:27093300). In vivo, when tested in fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death (PubMed:9417043, PubMed:12074021). Injection of this peptide together with the delta-conotoxin PVIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal 'fin-pop' in envenomed fish (PubMed:9417043, PubMed:12074021). When tested in mice, induces hyperactivity (PubMed:9417043).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Publication Abstract from PubMed

kappa-Conotoxin PVIIA from the venom of Conus purpurascens is the first cone snail toxin that was described to block potassium channels. We synthesized chemically this toxin and showed that its disulfide bridge pattern is similar to those of omega- and delta-conotoxins. kappa-conotoxin competes with radioactive alpha-dendrotoxin for binding to rat brain synaptosomes, confirming its capacity to bind to potassium channels; however, it behaves as a weak competitor. The three-dimensional structure of kappa-conotoxin PVIIA, as elucidated by NMR spectroscopy and molecular modeling, comprises two large parallel loops stabilized by a triple-stranded antiparallel beta-sheet and three disulfide bridges. The overall fold of kappa-conotoxin is similar to that of calcium channel-blocking omega-conotoxins but differs from those of potassium channel-blocking toxins from sea anemones, scorpions, and snakes. Local topographies of kappa-conotoxin PVIIA that might account for its capacity to recognize Kv1-type potassium channels are discussed.

Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails.,Savarin P, Guenneugues M, Gilquin B, Lamthanh H, Gasparini S, Zinn-Justin S, Menez A Biochemistry. 1998 Apr 21;37(16):5407-16. PMID:9548922^[7]

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

References

↑ Terlau H, Boccaccio A, Olivera BM, Conti F. The block of Shaker K+ channels by kappa-conotoxin PVIIA is state dependent. J Gen Physiol. 1999 Jul;114(1):125-40. PMID:10398696
↑ Jacobsen RB, Koch ED, Lange-Malecki B, Stocker M, Verhey J, Van Wagoner RM, Vyazovkina A, Olivera BM, Terlau H. Single amino acid substitutions in kappa-conotoxin PVIIA disrupt interaction with the shaker K+ channel. J Biol Chem. 2000 Aug 11;275(32):24639-44. doi: 10.1074/jbc.C900990199. PMID:10818087 doi:http://dx.doi.org/10.1074/jbc.C900990199
↑ Naranjo D. Inhibition of single Shaker K channels by kappa-conotoxin-PVIIA. Biophys J. 2002 Jun;82(6):3003-11. PMID:12023223 doi:http://dx.doi.org/S0006-3495(02)75641-5
↑ Terlau H, Shon KJ, Grilley M, Stocker M, Stuhmer W, Olivera BM. Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. PMID:12074021 doi:http://dx.doi.org/10.1038/381148a0
↑ Kwon S, Bosmans F, Kaas Q, Cheneval O, Conibear AC, Rosengren KJ, Wang CK, Schroeder CI, Craik DJ. Efficient enzymatic cyclization of an inhibitory cystine knot-containing peptide. Biotechnol Bioeng. 2016 Oct;113(10):2202-12. doi: 10.1002/bit.25993. Epub 2016, Aug 9. PMID:27093300 doi:http://dx.doi.org/10.1002/bit.25993
↑ Shon KJ, Stocker M, Terlau H, Stuhmer W, Jacobsen R, Walker C, Grilley M, Watkins M, Hillyard DR, Gray WR, Olivera BM. kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel. J Biol Chem. 1998 Jan 2;273(1):33-8. PMID:9417043
↑ Savarin P, Guenneugues M, Gilquin B, Lamthanh H, Gasparini S, Zinn-Justin S, Menez A. Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry. 1998 Apr 21;37(16):5407-16. PMID:9548922 doi:10.1021/bi9730341

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/1kcp"

@@ Line 1: / Line 1: @@
 ==3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES==
-<StructureSection load='1kcp' size='340' side='right'caption='[[1kcp]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
+<StructureSection load='1kcp' size='340' side='right'caption='[[1kcp]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conpu Conpu]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KCP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kcp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_purpurascens Conus purpurascens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KCP FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=1kcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kcp OCA], [https://pdbe.org/1kcp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kcp RCSB], [https://www.ebi.ac.uk/pdbsum/1kcp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kcp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CO17A_CONPU CO17A_CONPU]] Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the Shaker channel from insects. The interaction site between the Shaker channel and this toxin is within the S5-S6 loop of the Shaker channel. In fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death. Injection of this peptide together with the delta-conotoxin PVIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal "fin-pop" in envenomed fish. In mice, induces hyperactivity.<ref>PMID:10398696</ref> <ref>PMID:12023223</ref> <ref>PMID:12074021</ref> <ref>PMID:9417043</ref>
+[https://www.uniprot.org/uniprot/O17A_CONPU O17A_CONPU] Kappa-conotoxins bind and inhibit voltage-gated potassium channels (Kv). This toxin inhibits the drosophila Shaker channel (IC(50)=57-80 nM) (PubMed:12074021, PubMed:10818087, PubMed:27093300). In vivo, when tested in fish, this toxin induces hyperactivity, followed by continuous contraction and extension of major fins, without immobilization or death (PubMed:9417043, PubMed:12074021). Injection of this peptide together with the delta-conotoxin PVIA causes the sudden tetanus of prey (STOP) syndrome, which is a single, lethal 'fin-pop' in envenomed fish (PubMed:9417043, PubMed:12074021). When tested in mice, induces hyperactivity (PubMed:9417043).<ref>PMID:10398696</ref> <ref>PMID:10818087</ref> <ref>PMID:12023223</ref> <ref>PMID:12074021</ref> <ref>PMID:27093300</ref> <ref>PMID:9417043</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Conpu]]
+[[Category: Conus purpurascens]]
 [[Category: Large Structures]]
-[[Category: Gasparini, S]]
+[[Category: Gasparini S]]
-[[Category: Gilquin, B]]
+[[Category: Gilquin B]]
-[[Category: Guenneugues, M]]
+[[Category: Guenneugues M]]
-[[Category: Lamthanh, H]]
+[[Category: Lamthanh H]]
-[[Category: Menez, A]]
+[[Category: Menez A]]
-[[Category: Savarin, P]]
+[[Category: Savarin P]]
-[[Category: Zinn-Justin, S]]
+[[Category: Zinn-Justin S]]
-[[Category: Neurotoxin]]
-[[Category: Potassium channel inhibitor]]

1kcp

From Proteopedia

Revision as of 07:22, 18 May 2023

3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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