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2m01

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Solution structure of Kunitz-type neurotoxin LmKKT-1a from scorpion venom

Structural highlights

2m01 is a 1 chain structure with sequence from Lychas mucronatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

VKT21_LYCMC Dual-function toxin that completely inhibits trypsin activity at a molar ratio of 1:1 (Ki=140 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents (1 uM inhibits 50% of currents) (IC(50)=1.58 uM). Shows also weak inhibition on Kv1.1/KCNA1 (1 uM inhibits 25% of currents) and Kv1.2/KCNA2 (1 uM inhibits 25% of currents).^[1] ^[2]

Publication Abstract from PubMed

BACKGROUND: Recently, a new subfamily of long-chain toxins with a Kunitz-type fold was found in scorpion venom glands. Functionally, these toxins inhibit protease activity and block potassium channels. However, the genomic organization and three-dimensional (3-D) structure of this kind of scorpion toxin has not been reported. PRINCIPAL FINDINGS: Here, we characterized the genomic organization and 3-D nuclear magnetic resonance structure of the scorpion Kunitz-type toxin, LmKTT-1a, which has a unique cysteine pattern. The LmKTT-1a gene contained three exons, which were interrupted by two introns located in the mature peptide region. Despite little similarity to other Kunitz-type toxins and a unique pattern of disulfide bridges, LmKTT-1a possessed a conserved Kunitz-type structural fold with one alpha-helix and two beta-sheets. Comparison of the genomic organization, 3-D structure, and functional data of known toxins from the alpha-KTx, beta-KTx, gamma-KTx, and kappa-KTx subfamily suggested that scorpion Kunitz-type potassium channel toxins might have evolved from a new ancestor that is completely different from the common ancestor of scorpion toxins with a CSalpha/beta fold. Thus, these analyses provide evidence of a new scorpion potassium channel toxin subfamily, which we have named delta-KTx. CONCLUSIONS/SIGNIFICANCE: Our results highlight the genomic, structural, and evolutionary diversity of scorpion potassium channel toxins. These findings may accelerate the design and development of diagnostic and therapeutic peptide agents for human potassium channelopathies.

Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins.,Chen Z, Luo F, Feng J, Yang W, Zeng D, Zhao R, Cao Z, Liu M, Li W, Jiang L, Wu Y PLoS One. 2013;8(4):e60201. doi: 10.1371/journal.pone.0060201. Epub 2013 Apr 3. PMID:23573241^[3]

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

References

↑ Zhao R, Dai H, Qiu S, Li T, He Y, Ma Y, Chen Z, Wu Y, Li W, Cao Z. SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS One. 2011;6(11):e27548. doi: 10.1371/journal.pone.0027548. Epub 2011 Nov 8. PMID:22087336 doi:http://dx.doi.org/10.1371/journal.pone.0027548
↑ Chen ZY, Hu YT, Yang WS, He YW, Feng J, Wang B, Zhao RM, Ding JP, Cao ZJ, Li WX, Wu YL. Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem. 2012 Apr 20;287(17):13813-21. doi: 10.1074/jbc.M112.343996. Epub, 2012 Feb 21. PMID:22354971 doi:http://dx.doi.org/10.1074/jbc.M112.343996
↑ Chen Z, Luo F, Feng J, Yang W, Zeng D, Zhao R, Cao Z, Liu M, Li W, Jiang L, Wu Y. Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins. PLoS One. 2013;8(4):e60201. doi: 10.1371/journal.pone.0060201. Epub 2013 Apr 3. PMID:23573241 doi:http://dx.doi.org/10.1371/journal.pone.0060201

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/2m01"

@@ Line 1: / Line 1: @@
 ==Solution structure of Kunitz-type neurotoxin LmKKT-1a from scorpion venom==
-<StructureSection load='2m01' size='340' side='right' caption='[[2m01]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2m01' size='340' side='right'caption='[[2m01]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2m01]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buthus_sp._'vietnamese_brown_scorpion' Buthus sp. 'vietnamese brown scorpion']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M01 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2m01]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lychas_mucronatus Lychas mucronatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M01 FirstGlance]. <br>
-</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=2m01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m01 OCA], [http://pdbe.org/2m01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2m01 RCSB], [http://www.ebi.ac.uk/pdbsum/2m01 PDBsum]</span></td></tr>
+</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=2m01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m01 OCA], [https://pdbe.org/2m01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m01 RCSB], [https://www.ebi.ac.uk/pdbsum/2m01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m01 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/VPI1B_LYCMC VPI1B_LYCMC]] The recombinant protein has two functions. It completely inhibits trypsin activity at a molar ratio of 1:1 with a dissociation constant of 140 nM and also inhibits mKv1.3/KCNA3 potassium channel currents (1 uM inhibits 50% of currents).<ref>PMID:22087336</ref> <ref>PMID:22354971</ref>
+[https://www.uniprot.org/uniprot/VKT21_LYCMC VKT21_LYCMC] Dual-function toxin that completely inhibits trypsin activity at a molar ratio of 1:1 (Ki=140 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents (1 uM inhibits 50% of currents) (IC(50)=1.58 uM). Shows also weak inhibition on Kv1.1/KCNA1 (1 uM inhibits 25% of currents) and Kv1.2/KCNA2 (1 uM inhibits 25% of currents).<ref>PMID:22087336</ref> <ref>PMID:22354971</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Buthus sp. 'vietnamese brown scorpion']]
+[[Category: Large Structures]]
-[[Category: Chen, Z]]
+[[Category: Lychas mucronatus]]
-[[Category: Jiang, L]]
+[[Category: Chen Z]]
-[[Category: Liu, M]]
+[[Category: Jiang L]]
-[[Category: Luo, F]]
+[[Category: Liu M]]
-[[Category: Wu, Y]]
+[[Category: Luo F]]
-[[Category: Kunitz-type neurotoxin]]
+[[Category: Wu Y]]
-[[Category: Scorpion potassium channel toxin]]
-[[Category: Toxin]]

2m01

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Current revision

Solution structure of Kunitz-type neurotoxin LmKKT-1a from scorpion venom

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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