Target Information

General Information of This Target
Target ID
BTDT00043
Target Name
Potassium voltage-gated channel protein Shaker (Sh)
Target Bioclass
Transporter and channel
Uniprot ID
P08510
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
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Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Sh
Gene ID
32780
Synonym
mns; Protein minisleep
Sequence
MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQLQRNSLDGY
GSLPKLSSQDEEGGAGHGFGGGPQHFEPIPHDHDFCERVVINVSGLRFETQLRTLNQFPD
TLLGDPARRLRYFDPLRNEYFFDRSRPSFDAILYYYQSGGRLRRPVNVPLDVFSEEIKFY
ELGDQAINKFREDEGFIKEEERPLPDNEKQRKVWLLFEYPESSQAARVVAIISVFVILLS
IVIFCLETLPEFKHYKVFNTTTNGTKIEEDEVPDITDPFFLIETLCIIWFTFELTVRFLA
CPNKLNFCRDVMNVIDIIAIIPYFITLATVVAEEEDTLNLPKAPVSPQDKSSNQAMSLAI
LRVIRLVRVFRIFKLSRHSKGLQILGRTLKASMRELGLLIFFLFIGVVLFSSAVYFAEAG
SENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIVGSLCAIAGVLTIALPVPVIVSN
FNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPG
LTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQ
QNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV

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Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Forms rapidly inactivating tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient and may contribute to A- type currents. Plays a role in the regulation of sleep need or efficiency. Plays a role in sexual behavior, where it is important for male sex discrimination.

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Taxonomy ID
7227
TCDB ID
1.A.1.2.6
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Arthropoda
Class: Insecta
Order: Diptera
Family: Drosophilidae
Genus: Drosophila
Species: Drosophila melanogaster
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Conotoxin SIVA . . [1- 5]
 Toxin Info    Leiurotoxin-2 (I15L,D20C,M29I,R31G) Dissociation constant
0.14 nM
 [6]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 (S11G) Dissociation constant
0.834 nM
 [7]
 Toxin Info    AgTx2 (K32A) Dissociation constant
1.59 nM
 [7]
 Toxin Info    AgTx2 (T36A) Dissociation constant
2.23 nM
 [7]
 Toxin Info    AgTx2 (P37A) Dissociation constant
2.29 nM
 [7]
 Toxin Info    AgTx2_P37A Dissociation constant
4.71 nM
 [7]
 Toxin Info    OdK2 (G10V,S19K) Dissociation constant
5.3 nM
 [7]
 Toxin Info    Potassium channel toxin alpha-KTx 7.1 Dissociation constant
8.2 nM
 [8]
 Toxin Info    AgTx2_T36A Dissociation constant
13.64 nM
 [7]
 Toxin Info    AgTx2 (N30A) Dissociation constant
14.31 nM
 [7]
 Toxin Info    MTX (V1G,S2V,C3P,T4I,G5N,S6V,K7S,D8C,C9T,Y10G,C13Q,R14C,K15I,Q16K,T17P,G18C,C19K,P20D,N21A,A22G,K23M,C24R,I25F,N26G,S28C,C29M,K30N,C31R,Y32K,G33C,C34H) Dissociation constant
22.7 nM
 [7]
 Toxin Info    Potassium channel toxin alpha-KTx 6.1 Dissociation constant
32 nM
 [9]
 Toxin Info    Potassium channel toxin alpha-KTx 6.14 Dissociation constant
52 nM
 [10]
 Toxin Info    Potassium channel toxin alpha-KTx 13.1 Dissociation constant
65 nM
 [11]
 Toxin Info    Potassium channel toxin alpha-KTx 4.4 Dissociation constant
74 nM
 [12]
 Toxin Info    Potassium channel toxin alpha-KTx 6.17 Dissociation constant
82 nM
 [13]
 Toxin Info    ChTX (C19R) Dissociation constant
90 nM
 [14]
 Toxin Info    AgTx2 (M29A) Dissociation constant
95.41 nM
 [7]
 Toxin Info    Potassium channel toxin alpha-KTx 7.2 Dissociation constant
140 nM
 [8]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
160 nM
 [15- 26]
 Toxin Info    Potassium channel toxin alpha-KTx 2.2 Dissociation constant
160 nM
 [15- 26]
 Toxin Info    Potassium channel toxin alpha-KTx 13.3 Dissociation constant
200 nM
 [12]
 Toxin Info    Potassium channel toxin alpha-KTx 4.3 Dissociation constant
290 nM
 [27]
 Toxin Info    AgTx2 (G10V) Dissociation constant
508.1 nM
 [7]
 Toxin Info    AgTx2 (R31A) Dissociation constant
515.8 nM
 [7]
 Toxin Info    Potassium channel toxin alpha-KTx 24.1 Dissociation constant
540 nM
 [28]
 Toxin Info    Potassium channel toxin alpha-KTx 12.4 Dissociation constant
660 nM
 [29]
 Toxin Info    Potassium channel toxin alpha-KTx 12.2 Dissociation constant
660 nM
 [29]
 Toxin Info    Potassium channel toxin alpha-KTx 10.1 Dissociation constant
700 nM
 [30]
 Toxin Info    Potassium channel toxin alpha-KTx 18.2 Dissociation constant
1.5 μM
 [31]
 Toxin Info    Conorfamide-Sr3 Dissociation constant
2.7 μM
 [32], [33]
 Toxin Info    Conorfamide-Sr3 Dissociation constant
2.7 μM
 [32]
 Toxin Info    Potassium channel toxin alpha-KTx 12.3 Dissociation constant
3 μM
 [34]
 Toxin Info    Potassium channel toxin alpha-KTx 13.4 Dissociation constant
3 μM
 [35]
 Toxin Info    Potassium channel toxin alpha-KTx 10.2 Dissociation constant
4.1 μM
 [30]
 Toxin Info    Potassium channel toxin alpha-KTx 18.1 Dissociation constant
4.7 μM
 [12]
 Toxin Info    Potassium channel toxin alpha-KTx 3.4 Inhibition constant
0.16 nM
 [36]
 Toxin Info    Potassium channel toxin alpha-KTx 3.2 Inhibition constant
0.64 nM
 [36]
 Toxin Info    Potassium channel toxin alpha-KTx 3.3 Inhibition constant
0.64 nM
 [36]
 Toxin Info    Kappa-stichotoxin-Hmg1a Inhibition constant
1 nM
 [37]
 Toxin Info    Kappa-stichotoxin-She3a Inhibition constant
2 nM
 [37]
 Toxin Info    Potassium channel toxin HmK (S34T) Inhibition constant
3.9 nM
 [37]
 Toxin Info    Potassium channel toxin alpha-KTx 1.1 Inhibition constant
227 nM
 [36]
 Toxin Info    Kappa-actitoxin-Aer3a Inhibition constant
445 nM
 [37]
 Toxin Info    CGX-1052 Inhibition rate . [38]
 Toxin Info    CGX-1053 Inhibition rate . [38]
 Toxin Info    CGX-1054 Inhibition rate . [38]
 Toxin Info    CGX-1055 Inhibition rate . [38]
 Toxin Info    CGX-1056 Inhibition rate . [38]
 Toxin Info    CGX-1057 Inhibition rate . [38]
 Toxin Info    CGX-1058 Inhibition rate . [38]
 Toxin Info    CGX-1059 Inhibition rate . [38]
 Toxin Info    Calcium channel toxin-like peptide-1 Inhibition rate . [39]
 Toxin Info    Kunitz-type serine protease inhibitor homolog delta-dendrotoxin Inhibition rate . [40]
 Toxin Info    Potassium channel toxin alpha-KTx 20.1 Inhibition rate . [41]
 Toxin Info    Potassium channel toxin alpha-KTx 3.11 Inhibition rate . [42]
 Toxin Info    Potassium channel toxin alpha-KTx 6.5 Inhibition rate . [43]
 Toxin Info    Potassium channel toxin alpha-KTx 8.5 Inhibition rate . [44]
 Toxin Info    Potassium channel toxin kappa-KTx 2.5 Inhibition rate . [45]
 Toxin Info    Potassium channel toxin kappa-KTx 2.9 Inhibition rate . [28]
 Toxin Info    Potassium channel toxin alpha-KTx 16.4 Inhibition rate . [46]
 Toxin Info    KappaPI-actitoxin-Ael3a Inhibition rate . [47], [48]
 Toxin Info    CGX-1051 Inhibition rate . [38]
 Toxin Info    Fin-popping peptide (P4A,A5N) Inhibition rate . [38]
 Toxin Info    Fin-popping peptide (R2A,A5N) Inhibition rate . [38]
 Toxin Info    Potassium channel toxin alpha-KTx 21.1 Inhibition rate
20 %
 [49]
 Toxin Info    Potassium channel toxin alpha-KTx 6.12 Inhibition rate
20 %
 [50]
 Toxin Info    Potassium channel toxin alpha-KTx 3.6 Inhibition rate
21 %
 [51]
 Toxin Info    Potassium channel toxin alpha-KTx 8.2 Inhibition rate
70 %
 [52]
 Toxin Info    Potassium channel toxin alpha-KTx 12.1 Inhibition rate
80 %
 [53]
 Toxin Info    Kappa-buthitoxin-Tt2b Inhibition rate
88 %
 [54]
 Toxin Info    Potassium channel toxin alpha-KTx 4.1 Inhibition rate
97 %
 [53]
 Toxin Info    Potassium channel toxin alpha-KTx 6.2 IC50
2.4 nM
 [55]
 Toxin Info    Potassium channel toxin alpha-KTx 6.4 IC50
3 nM
 [56]
 Toxin Info    Potassium channel toxin alpha-KTx 3.10 IC50
3.5 nM
 [57]
 Toxin Info    Kappa-conotoxin PVIIA IC50
60 nM
 [38- 68]
 Toxin Info    CGX-1060 IC50
69 nM
 [38]
 Toxin Info    CGX-1061 IC50
82 nM
 [38]
 Toxin Info    CGX-1062 IC50
86 nM
 [38]
 Toxin Info    CGX-1063 IC50
170 nM
 [38]
 Toxin Info    CGX-1064 IC50
183 nM
 [38]
 Toxin Info    CGX-1065 IC50
189 nM
 [38]
 Toxin Info    CGX-1066 IC50
199 nM
 [38]
 Toxin Info    CGX-1067 IC50
276 nM
 [38]
 Toxin Info    Kunitz-type conkunitzin-S1 IC50
502 nM
 [69], [70], [71]
 Toxin Info    CGX-1068 IC50
639 nM
 [38]
 Toxin Info    CGX-1069 IC50
745 nM
 [38]
 Toxin Info    CGX-1070 IC50
993 nM
 [38]
 Toxin Info    Fin-popping peptide (N24A_A25K) IC50
1.066 μM
 [38]
 Toxin Info    Potassium channel toxin alpha-KTx 8.6 IC50
3 μM
 [52]
 Toxin Info    Potassium channel toxin alpha-KTx 15.1 IC50
4.5 μM
 [72]
 Toxin Info    Potassium channel toxin alpha-KTx 9.2 IC50
4.64 μM
 [73]
 Toxin Info    CGX-1071 IC50
6.663 μM
 [38]
 Toxin Info    Neurotoxin lambda-MeuTx IC50
12.3 μM
 [39]
 Toxin Info    Potassium channel toxin alpha-KTx 9.1 IC50
20.44 μM
 [73]
References
Ref 1 cDNA cloning of two A-superfamily conotoxins from Conus striatus. Toxicon. 2003 Nov;42(6):613-9. doi: 10.1016/j.toxicon.2003.08.005.
Ref 2 The A-superfamily of conotoxins: structural and functional divergence. J Biol Chem. 2004 Apr 23;279(17):17596-606. doi: 10.1074/jbc.M309654200. Epub 2003 Dec 30.
Ref 3 Two toxins from Conus striatus that individually induce tetanic paralysis. Biochemistry. 2006 Nov 28;45(47):14212-22. doi: 10.1021/bi061485s.
Ref 4 Analysis of expressed sequence tags from the venom ducts of Conus striatus: focusing on the expression profile of conotoxins. Biochimie. 2006 Feb;88(2):131-40. doi: 10.1016/j.biochi.2005.08.001. Epub 2005 Sep 8.
Ref 5 An O-glycosylated neuroexcitatory conus peptide. Biochemistry. 1998 Nov 17;37(46):16019-25. doi: 10.1021/bi981690a.
Ref 6 Contribution of the S4 segment to gating charge in the Shaker K+ channel. Neuron. 1996 Jun;16(6):1169-77. doi: 10.1016/s0896-6273(00)80143-9.
Ref 7 Spatial localization of the K+ channel selectivity filter by mutant cycle-based structure analysis. Neuron. 1996 Jan;16(1):131-9. doi: 10.1016/s0896-6273(00)80030-6.
Ref 8 Two novel toxins from the venom of the scorpion Pandinus imperator show that the N-terminal amino acid sequence is important for their affinities towards Shaker B K+ channels. J Membr Biol. 1996 Jul;152(1):49-56. doi: 10.1007/s002329900084.
Ref 9 Block of ShakerB K+ channels by Pi1, a novel class of scorpion toxin. FEBS Lett. 1997 Jan 3;400(2):197-200. doi: 10.1016/s0014-5793(96)01387-7.
Ref 10 HgeTx1, the first K+-channel specific toxin characterized from the venom of the scorpion Hadrurus gertschi Soleglad. Toxicon. 2006 Dec 15;48(8):1046-53. doi: 10.1016/j.toxicon.2006.08.009. Epub 2006 Sep 5.
Ref 11 Tc1, from Tityus cambridgei, is the first member of a new subfamily of scorpion toxin that blocks K(+)-channels. FEBS Lett. 2000 Dec 8;486(2):117-20. doi: 10.1016/s0014-5793(00)02253-5.
Ref 12 Two novel toxins from the Amazonian scorpion Tityus cambridgei that block Kv1.3 and Shaker B K(+)-channels with distinctly different affinities. Biochim Biophys Acta. 2002 Dec 16;1601(2):123-31. doi: 10.1016/s1570-9639(02)00458-2.
Ref 13 OcyKTx2, a new K?-channel toxin characterized from the venom of the scorpion Opisthacanthus cayaporum. Peptides. 2013 Aug;46:40-6. doi: 10.1016/j.peptides.2013.04.021. Epub 2013 May 15.
Ref 14 Engineering a uniquely reactive thiol into a cysteine-rich peptide. Protein Eng. 1994 Apr;7(4):503-7. doi: 10.1093/protein/7.4.503.
Ref 15 Synthesis of Novel cis-2-Azetidinones from imines and aclychloride using triethylamine. Acta Chim Slov. 2023 Dec 4;70(4):628-633. doi: 10.17344/acsi.2023.8451.
Ref 16 Backward-Eulerian Footprint Modelling Based on the Adjoint Equation for Atmospheric and Urban-Terrain Dispersion. Boundary Layer Meteorol. 2023;188(1):159-183. doi: 10.1007/s10546-023-00807-z. Epub 2023 Apr 17.
Ref 17 Leaf spot on Alocasia macrorrhizos caused by Fusarium asiaticum in Sichuan, China. Plant Dis. 2022 Sep 11. doi: 10.1094/PDIS-04-22-0844-PDN. Online ahead of print.
Ref 18 Incidence and predictors of chronic kidney disease in type-II diabetes mellitus patients attending at the Amhara region referral hospitals, Ethiopia: A follow-up study. PLoS One. 2022 Jan 26;17(1):e0263138. doi: 10.1371/journal.pone.0263138. eCollection 2022.
Ref 19 A Method for More Accurate Determination of Resonance Frequency of the Cardiovascular System, and Evaluation of a Program to Perform It. Appl Psychophysiol Biofeedback. 2022 Mar;47(1):17-26. doi: 10.1007/s10484-021-09524-0. Epub 2021 Oct 16.
Ref 20 First Report of Fusarium wilt of Coleus forskohlii Caused by Fusarium oxysporum in China. Plant Dis. 2021 Jan 26. doi: 10.1094/PDIS-11-20-2489-PDN. Online ahead of print.
Ref 21 Shock waves from the inhomogeneous Boltzmann equation. Phys Rev E. 2019 Dec;100(6-1):062120. doi: 10.1103/PhysRevE.100.062120.
Ref 22 Classifying Changes to Preventive Interventions: Applying Adaptation Taxonomies. J Prim Prev. 2019 Feb;40(1):89-109. doi: 10.1007/s10935-018-00531-2.
Ref 23 Quantification of the passive and active biaxial mechanical behaviour and microstructural organization of rat thoracic ducts. J R Soc Interface. 2015 Jul 6;12(108):20150280. doi: 10.1098/rsif.2015.0280.
Ref 24 A model of mechanical interactions between heart and lungs. Philos Trans A Math Phys Eng Sci. 2009 Dec 13;367(1908):4741-57. doi: 10.1098/rsta.2009.0137.
Ref 25 Experimental test of nonlocal realistic theories without the rotational symmetry assumption. Phys Rev Lett. 2007 Nov 23;99(21):210406. doi: 10.1103/PhysRevLett.99.210406. Epub 2007 Nov 21.
Ref 26 Structures and phase transitions of the A7PSe6 (A = ag, Cu) argyrodite-type ionic conductors. III. alpha-Cu7PSe6. Acta Crystallogr B. 2000 Dec;56 (Pt 6):972-9. doi: 10.1107/s0108768100010260.
Ref 27 A novel K+ channel blocking toxin from Tityus discrepans scorpion venom. FEBS Lett. 1999 Jul 30;456(1):146-8. doi: 10.1016/s0014-5793(99)00947-3.
Ref 28 Pi5 and Pi6, two undescribed peptides from the venom of the scorpion Pandinus imperator and their effects on K(+)-channels. Toxicon. 2017 Jul;133:136-144. doi: 10.1016/j.toxicon.2017.05.011. Epub 2017 May 11.
Ref 29 Disulfide bridges and blockage of Shaker B K(+)-channels by another butantoxin peptide purified from the Argentinean scorpion Tityus trivittatus. Toxicon. 2003 Feb;41(2):173-9. doi: 10.1016/s0041-0101(02)00247-7.
Ref 30 Cobatoxins 1 and 2 from Centruroides noxius Hoffmann constitute a subfamily of potassium-channel-blocking scorpion toxins. Eur J Biochem. 1998 Jun 15;254(3):468-79. doi: 10.1046/j.1432-1327.1998.2540468.x.
Ref 31 Proteomic analysis of Tityus discrepans scorpion venom and amino acid sequence of novel toxins. Proteomics. 2006 Jun;6(12):3718-27. doi: 10.1002/pmic.200500525.
Ref 32 Conorfamide-Sr3, a structurally novel specific inhibitor of the Shaker K(+) channel. Toxicon. 2017 Nov;138:53-58. doi: 10.1016/j.toxicon.2017.07.024. Epub 2017 Jul 31.
Ref 33 Studies of Conorfamide-Sr3 on Human Voltage-Gated Kv1 Potassium Channel Subtypes. Mar Drugs. 2020 Aug 13;18(8):425. doi: 10.3390/md18080425.
Ref 34 The Brazilian scorpion Tityus costatus Karsch: genes, peptides and function. Toxicon. 2005 Mar 1;45(3):273-83. doi: 10.1016/j.toxicon.2004.10.014. Epub 2004 Dec 10.
Ref 35 Proteomic analysis of the venom from the scorpion Tityus stigmurus: biochemical and physiological comparison with other Tityus species. Comp Biochem Physiol C Toxicol Pharmacol. 2007 Jul-Aug;146(1-2):147-157. doi: 10.1016/j.cbpc.2006.12.004. Epub 2006 Dec 16.
Ref 36 Purification and characterization of three inhibitors of voltage-dependent K+ channels from Leiurus quinquestriatus var. hebraeus venom. Biochemistry. 1994 Jun 7;33(22):6834-9. doi: 10.1021/bi00188a012.
Ref 37 Designer and natural peptide toxin blockers of the KcsA potassium channel identified by phage display. Proc Natl Acad Sci U S A. 2015 Dec 15;112(50):E7013-21. doi: 10.1073/pnas.1514728112. Epub 2015 Dec 1.
Ref 38 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.
Ref 39 Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold. Biosci Rep. 2013 Jun 27;33(3):e00047. doi: 10.1042/BSR20130052.
Ref 40 A snake toxin inhibitor of inward rectifier potassium channel ROMK1. Biochemistry. 1998 Oct 20;37(42):14867-74. doi: 10.1021/bi980929k.
Ref 41 A novel toxin from the venom of the scorpion Tityus trivittatus, is the first member of a new alpha-KTX subfamily. FEBS Lett. 2006 Jan 23;580(2):592-6. doi: 10.1016/j.febslet.2005.12.073. Epub 2006 Jan 4.
Ref 42 OdK2, a Kv1.3 channel-selective toxin from the venom of the Iranian scorpion Odonthobuthus doriae. Toxicon. 2008 Jun 15;51(8):1424-30. doi: 10.1016/j.toxicon.2008.03.027. Epub 2008 Mar 29.
Ref 43 Two similar peptides from the venom of the scorpion Pandinus imperator, one highly effective blocker and the other inactive on K+ channels. Toxicon. 1998 May;36(5):759-70. doi: 10.1016/s0041-0101(97)00163-3.
Ref 44 The first potassium channel toxin from the venom of the Iranian scorpion Odonthobuthus doriae. FEBS Lett. 2006 Nov 13;580(26):6254-8. doi: 10.1016/j.febslet.2006.10.029. Epub 2006 Oct 20.
Ref 45 The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum. Peptides. 2011 Jul;32(7):1509-17. doi: 10.1016/j.peptides.2011.05.017. Epub 2011 May 23.
Ref 46 Molecular divergence of two orthologous scorpion toxins affecting potassium channels. Comp Biochem Physiol A Mol Integr Physiol. 2011 Jul;159(3):313-21. doi: 10.1016/j.cbpa.2011.03.027. Epub 2011 Apr 3.
Ref 47 A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties. Biochem Pharmacol. 2011 Jul 1;82(1):81-90. doi: 10.1016/j.bcp.2011.03.023. Epub 2011 Apr 6.
Ref 48 Development of a rational nomenclature for naming peptide and protein toxins from sea anemones. Toxicon. 2012 Sep 15;60(4):539-50. doi: 10.1016/j.toxicon.2012.05.020. Epub 2012 Jun 5.
Ref 49 Purification and characterization of Ts15, the first member of a new -KTX subfamily from the venom of the Brazilian scorpion Tityus serrulatus. Toxicon. 2011 Jul;58(1):54-61. doi: 10.1016/j.toxicon.2011.05.001. Epub 2011 May 13.
Ref 50 Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes. Mol Pharmacol. 2005 Apr;67(4):1034-44. doi: 10.1124/mol.104.007187. Epub 2004 Dec 22.
Ref 51 A potent potassium channel blocker from Mesobuthus eupeus scorpion venom. Biochimie. 2010 Dec;92(12):1847-53. doi: 10.1016/j.biochi.2010.08.003. Epub 2010 Aug 14.
Ref 52 Molecular diversity and functional evolution of scorpion potassium channel toxins. Mol Cell Proteomics. 2011 Feb;10(2):M110.002832. doi: 10.1074/mcp.M110.002832. Epub 2010 Sep 30.
Ref 53 Electrophysiological characterization of Ts6 and Ts7, K? channel toxins isolated through an improved Tityus serrulatus venom purification procedure. Toxins (Basel). 2014 Feb 28;6(3):892-913. doi: 10.3390/toxins6030892.
Ref 54 New tricks of an old pattern: structural versatility of scorpion toxins with common cysteine spacing. J Biol Chem. 2012 Apr 6;287(15):12321-30. doi: 10.1074/jbc.M111.329607. Epub 2012 Jan 10.
Ref 55 Effect of maurotoxin, a four disulfide-bridged toxin from the chactoid scorpion Scorpio maurus, on Shaker K+ channels. J Pept Res. 2000 Jun;55(6):419-27. doi: 10.1034/j.1399-3011.2000.00715.x.
Ref 56 Synthesis and characterization of Pi4, a scorpion toxin from Pandinus imperator that acts on K+ channels. Eur J Biochem. 2003 Sep;270(17):3583-92. doi: 10.1046/j.1432-1033.2003.03743.x.
Ref 57 Isolation of the first toxin from the scorpion Buthus occitanus israelis showing preference for Shaker potassium channels. FEBS Lett. 2007 May 29;581(13):2478-84. doi: 10.1016/j.febslet.2007.04.065. Epub 2007 Apr 30.
Ref 58 kappa-Conotoxin PVIIA is a peptide inhibiting the shaker K+ channel. J Biol Chem. 1998 Jan 2;273(1):33-8. doi: 10.1074/jbc.273.1.33.
Ref 59 Strategy for rapid immobilization of prey by a fish-hunting marine snail. Nature. 1996 May 9;381(6578):148-51. doi: 10.1038/381148a0.
Ref 60 The block of Shaker K+ channels by kappa-conotoxin PVIIA is state dependent. J Gen Physiol. 1999 Jul;114(1):125-40. doi: 10.1085/jgp.114.1.125.
Ref 61 Molecular simulation of the interaction of kappa-conotoxin-PVIIA with the Shaker potassium channel pore. Eur Biophys J. 2001 Dec;30(7):528-36. doi: 10.1007/s00249-001-0189-8.
Ref 62 Inhibition of single Shaker K channels by kappa-conotoxin-PVIIA. Biophys J. 2002 Jun;82(6):3003-11. doi: 10.1016/S0006-3495(02)75641-5.
Ref 63 Electrostatic recognition and induced fit in the kappa-PVIIA toxin binding to Shaker potassium channel. J Am Chem Soc. 2005 May 11;127(18):6836-49. doi: 10.1021/ja042641q.
Ref 64 Postischemic administration of CGX-1051, a peptide from cone snail venom, reduces infarct size in both rat and dog models of myocardial ischemia and reperfusion. J Cardiovasc Pharmacol. 2005 Aug;46(2):141-6. doi: 10.1097/01.fjc.0000167015.84715.27.
Ref 65 Why the Drosophila Shaker K+ channel is not a good model for ligand binding to voltage-gated Kv1 channels. Biochemistry. 2013 Mar 5;52(9):1631-40. doi: 10.1021/bi301257p. Epub 2013 Feb 20.
Ref 66 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.
Ref 67 Solution structure and proposed binding mechanism of a novel potassium channel toxin kappa-conotoxin PVIIA. Structure. 1997 Dec 15;5(12):1585-97. doi: 10.1016/s0969-2126(97)00307-9.
Ref 68 Three-dimensional structure of kappa-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry. 1998 Apr 21;37(16):5407-16. doi: 10.1021/bi9730341.
Ref 69 Production of recombinant Conkunitzin-S1 in Escherichia coli. Protein Expr Purif. 2006 Jun;47(2):640-4. doi: 10.1016/j.pep.2006.01.019. Epub 2006 Feb 20.
Ref 70 Conkunitzin-S1 is the first member of a new Kunitz-type neurotoxin family. Structural and functional characterization. J Biol Chem. 2005 Jun 24;280(25):23766-70. doi: 10.1074/jbc.C500064200. Epub 2005 Apr 15.
Ref 71 Structure of conkunitzin-S1, a neurotoxin and Kunitz-fold disulfide variant from cone snail. Acta Crystallogr D Biol Crystallogr. 2006 Sep;62(Pt 9):980-90. doi: 10.1107/S0907444906021123. Epub 2006 Aug 19.
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