1wz5

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of Pi1-3p

Structural highlights

1wz5 is a 1 chain structure with sequence from Pandinus imperator. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KAX61_PANIM Potently and reversibly inhibits the insect voltage-gated Shaker (Sh) potassium channel (isoform alpha (B)), the mammalian voltage-gated potassium channels Kv1.2/KCNA2. Its effect on Kv1.3/KCNA3 is controversial, since this channel is voltage-independently inhibited in PubMed:9464266, but is not affected in PubMed:10931199. Furthermore, this toxin competes with apamin (a small conductance calcium-activated potassium channel inhibitor) for binding onto rat brain synaptosomes.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Animal toxins are highly reticulated and structured polypeptides that adopt a limited number of folds. In scorpion species, the most represented fold is the alpha/beta scaffold in which an helical structure is connected to an antiparallel beta-sheet by two disulfide bridges. The intimate relationship existing between peptide reticulation and folding remains poorly understood. Here, we investigated the role of disulfide bridging on the 3D structure of HsTx1, a scorpion toxin potently active on Kv1.1 and Kv1.3 channels. This toxin folds along the classical alpha/beta scaffold but belongs to a unique family of short-chain, four disulfide-bridged toxins. Removal of the fourth disulfide bridge of HsTx1 does not affect its helical structure, whereas its two-stranded beta-sheet is altered from a twisted to a nontwisted configuration. This structural change in HsTx1 is accompanied by a marked decrease in Kv1.1 and Kv1.3 current blockage, and by alterations in the toxin to channel molecular contacts. In contrast, a similar removal of the fourth disulfide bridge of Pi1, another scorpion toxin from the same structural family, has no impact on its 3D structure, pharmacology, or channel interaction. These data highlight the importance of disulfide bridging in reaching the correct bioactive conformation of some toxins.

The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily.,Carrega L, Mosbah A, Ferrat G, Beeton C, Andreotti N, Mansuelle P, Darbon H, De Waard M, Sabatier JM Proteins. 2005 Dec 1;61(4):1010-23. PMID:16247791^[5]

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

References

↑ Fajloun Z, Carlier E, Lecomte C, Geib S, Di Luccio E, Bichet D, Mabrouk K, Rochat H, De Waard M, Sabatier JM. Chemical synthesis and characterization of Pi1, a scorpion toxin from Pandinus imperator active on K+ channels. Eur J Biochem. 2000 Aug;267(16):5149-55. PMID:10931199
↑ Olamendi-Portugal T, Gomez-Lagunas F, Gurrola GB, Possani LD. A novel structural class of K+-channel blocking toxin from the scorpion Pandinus imperator. Biochem J. 1996 May 1;315 ( Pt 3):977-81. PMID:8645186
↑ Gomez-Lagunas F, Olamendi-Portugal T, Possani LD. Block of ShakerB K+ channels by Pi1, a novel class of scorpion toxin. FEBS Lett. 1997 Jan 3;400(2):197-200. PMID:9001397
↑ Peter M Jr, Varga Z, Panyi G, Bene L, Damjanovich S, Pieri C, Possani LD, Gaspar R Jr. Pandinus imperator scorpion venom blocks voltage-gated K+ channels in human lymphocytes. Biochem Biophys Res Commun. 1998 Jan 26;242(3):621-5. PMID:9464266 doi:http://dx.doi.org/10.1006/bbrc.1997.8018
↑ Carrega L, Mosbah A, Ferrat G, Beeton C, Andreotti N, Mansuelle P, Darbon H, De Waard M, Sabatier JM. The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily. Proteins. 2005 Dec 1;61(4):1010-23. PMID:16247791 doi:10.1002/prot.20681

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/1wz5"

Categories: Large Structures | Pandinus imperator | Ferrat G

@@ Line 1: / Line 1: @@
 ==Solution structure of Pi1-3p==
-<StructureSection load='1wz5' size='340' side='right'caption='[[1wz5]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
+<StructureSection load='1wz5' size='340' side='right'caption='[[1wz5]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1wz5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pandinus_imperator Pandinus imperator]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ5 FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</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=1wz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz5 OCA], [https://pdbe.org/1wz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/KAX61_PANIM KAX61_PANIM]] Potently and reversibly inhibits the insect voltage-gated Shaker (Sh) potassium channel (isoform alpha (B)), the mammalian voltage-gated potassium channels Kv1.2/KCNA2. Its effect on Kv1.3/KCNA3 is controversial, since this channel is voltage-independently inhibited in PubMed:9464266, but is not affected in PubMed:10931199. Furthermore, this toxin competes with apamin (a small conductance calcium-activated potassium channel inhibitor) for binding onto rat brain synaptosomes.<ref>PMID:10931199</ref> <ref>PMID:8645186</ref> <ref>PMID:9001397</ref> <ref>PMID:9464266</ref>
+[https://www.uniprot.org/uniprot/KAX61_PANIM KAX61_PANIM] Potently and reversibly inhibits the insect voltage-gated Shaker (Sh) potassium channel (isoform alpha (B)), the mammalian voltage-gated potassium channels Kv1.2/KCNA2. Its effect on Kv1.3/KCNA3 is controversial, since this channel is voltage-independently inhibited in PubMed:9464266, but is not affected in PubMed:10931199. Furthermore, this toxin competes with apamin (a small conductance calcium-activated potassium channel inhibitor) for binding onto rat brain synaptosomes.<ref>PMID:10931199</ref> <ref>PMID:8645186</ref> <ref>PMID:9001397</ref> <ref>PMID:9464266</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 27: / Line 28: @@
 [[Category: Large Structures]]
 [[Category: Pandinus imperator]]
-[[Category: Ferrat, G]]
+[[Category: Ferrat G]]
-[[Category: Ionic channel inhibitor]]
-[[Category: Toxin]]

1wz5

From Proteopedia

Current revision

Solution structure of Pi1-3p

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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