Target Information

General Information of This Target
Target ID
BTDT00036
Target Name
Sodium channel protein type 2 subunit alpha (Scn2a)
Target Bioclass
Transporter and channel
Uniprot ID
P04775
3D Structure
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2D Sequence
3D Structure
Source
Predict by Alphafold2
?
Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Scn2a
Gene ID
24766
Synonym
Scn2a1; Sodium channel protein brain II subunit alpha; Sodium channel protein type II subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.2
Sequence
MARSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGK
SLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRK
LAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFC
LEDFTFLRNPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGA
LIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSL
DWNGTAFNRTVNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNP
NYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLI
LAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGI
GVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFQFS
LEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFNFKGRVKDIGSENDFADDEHST
FEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGP
SALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPSRQRAMSMASILTNTMEELEE
SRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEH
YPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGL
ANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGM
QLFGKSYKECVCKISNDCELPRWHMHHFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCL
TVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRK
IREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGS
SVEKYVVDESDYMSFINNPSLTVTVPIALGESDFENLNTEEFSSESDMEESKEKLNATSS
SEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKT
CYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLK
WVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRF
EGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVV
NNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQ
PKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNA
MKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMT
NILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFV
SPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMS
NFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGS
SVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYE
VWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFA
FTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYL
LKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTK
PEKEKFEKDKSEKEDKGKDIRESKK

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Family
the sodium channel (TC 1.A.1.10) family
Function
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory.

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Taxonomy ID
10116
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Rattus
Species: Rattus norvegicus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Mu-conotoxin SmIIIA Dissociation constant
1.3 nM
 [1- 5]
 Toxin Info    Mu-conotoxin BuIIIB Dissociation constant
13 nM
 [2- 9]
 Toxin Info    N.vectensis toxin 4 Effect . [10]
 Toxin Info    N.vectensis toxin 5 Effect . [10]
 Toxin Info    Potassium channel toxin AbeTx1 Inhibition rate . [11]
 Toxin Info    U3-agatoxin-Ao1f Inhibition rate . [12], [13]
 Toxin Info    Alpha-mammal toxin AaH2 Effective concentration 50
2.6 nM
 [14- 23]
 Toxin Info    Nemertide alpha-6 Effective concentration 50
7.9 nM
 [24], [25]
 Toxin Info    Alpha-toxin Amm8 Effective concentration 50
29 nM
 [17- 28]
 Toxin Info    Nemertide alpha-4 Effective concentration 50
92 nM
 [24], [25]
 Toxin Info    Nemertide alpha-2 Effective concentration 50
97.9 nM
 [24], [25]
 Toxin Info    Nemertide alpha-5 Effective concentration 50
102.1 nM
 [24], [25]
 Toxin Info    APETx2 Effective concentration 50
114 nM
 [29- 38]
 Toxin Info    Nemertide alpha-2 Effective concentration 50
125.8 nM
 [24], [25]
 Toxin Info    Nemertide alpha-3 Effective concentration 50
125.8 nM
 [24], [25]
 Toxin Info    Nemertide alpha-3 Effective concentration 50
125.8 nM
 [24], [25]
 Toxin Info    Nemertide alpha-7 Effective concentration 50
171.5 nM
 [24], [25]
 Toxin Info    Nemertide alpha-1 Effective concentration 50
359.6 nM
 [24- 39]
 Toxin Info    Nemertide alpha-1 Effective concentration 50
359.6 nM
 [24- 39]
 Toxin Info    Neurotoxin BmK-M11 Effective concentration 50
>30 μM
 [40], [41], [42]
 Toxin Info    Delta-conotoxin GmVIA Effective concentration 50
2.5 μM
 [43], [44], [45]
 Toxin Info    Delta-conotoxin PVIA Effective concentration 50
2.9 μM
 [46], [47], [45], [48]
 Toxin Info    HWTX-IV IC50
˜150 nM
 [49]
 Toxin Info    TIIIA IC50
0.5 nM
 [50]
 Toxin Info    SA-III[desN5,G6;D15A]SIIIA (320) IC50
3.2 nM
 [50]
 Toxin Info    SIIIA 220 D15A IC50
5 nM
 [50]
 Toxin Info    Mu-conotoxin SIIIB IC50
5 nM
 [51], [52]
 Toxin Info    SA-I[D15A]SIIIA(3-20) IC50
5.9 nM
 [50]
 Toxin Info    SB-I[N5K=D15A]SIIIA (3-20) IC50
8.2 nM
 [50]
 Toxin Info    SIIIA IC50
9.6 nM
 [50]
 Toxin Info    SA-II[desG6,D15A]SIIIA(3-20) IC50
12 nM
 [50]
 Toxin Info    SB-III[N5K desG6,G7;D15A]SIIIA (320) IC50
26.4 nM
 [50]
 Toxin Info    Mu-conotoxin TIIIA IC50
40 nM
 [2- 53]
 Toxin Info    Mu-conotoxin SIIIC IC50
40 nM
 [53]
 Toxin Info    SB-II[N5K,desG6,D15A] SIIIA (3-20) IC50
50 nM
 [50]
 Toxin Info    Mu-conotoxin MrVIA IC50
532 nM
 [45- 58]
 Toxin Info    Mu-conotoxin PIIIA IC50
620 nM
 [2- 62]
 Toxin Info    Delta-theraphotoxin-Cg1a 2 IC50
870 nM
 [63- 69]
 Toxin Info    Delta-theraphotoxin-Cg1a 3 IC50
870 nM
 [63- 69]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 IC50
870 nM
 [64- 70]
 Toxin Info    PnM9 IC50
0.3 ± 0.01 μM
 [71]
 Toxin Info    PnCS4 IC50
0.8 ± 0.1 μM
 [71]
 Toxin Info    O-MrVIB IC50
1 μM
 [72]
 Toxin Info    Mu-conotoxin SxIIIA IC50
1 μM
 [2- 73]
 Toxin Info    PnCS2 IC50
1.0 ± 0.1 μM
 [71]
 Toxin Info    PnM2 IC50
1.8 ± 0.5 μM
 [71]
 Toxin Info    Mu-conotoxin GIIIA IC50
2.7 - 17.8 μM
 [2- 84]
 Toxin Info    PnM8 IC50
3.7 ± 0.2 μM
 [71]
 Toxin Info    PnM5 IC50
4.2 ± 0.4 μM
 [71]
 Toxin Info    PnCS3 IC50
5.3 ± 0.3 μM
 [71]
 Toxin Info    PnM1 IC50
6.4 ± 0.2 μM
 [71]
 Toxin Info    PnM7 IC50
7.2 ± 0.1 μM
 [71]
 Toxin Info    PnM6 IC50
31.7 ± 2.1 μM
 [71]
 Toxin Info    Pn IC50
53.7 ± 3.2 μM
 [71]
 Toxin Info    Mu-theraphotoxin-Hhn2b 1 IC50
68 μM
 [85], [86], [87], [88]
 Toxin Info    Mu-theraphotoxin-Hhn2b 2 IC50
68 μM
 [85], [86], [87], [88]
 Toxin Info    Mu-theraphotoxin-Hhn2b 3 IC50
68 μM
 [85], [86], [87], [88]
References
Ref 1 Mu-conotoxin SmIIIA, a potent inhibitor of tetrodotoxin-resistant sodium channels in amphibian sympathetic and sensory neurons. Biochemistry. 2002 Dec 24;41(51):15388-93. doi: 10.1021/bi0265628.
Ref 2 -Conotoxins that differentially block sodium channels NaV1.1 through 1.8 identify those responsible for action potentials in sciatic nerve. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10302-7. doi: 10.1073/pnas.1107027108. Epub 2011 Jun 7.
Ref 3 A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors. Br J Pharmacol. 2012 Jul;166(5):1654-68. doi: 10.1111/j.1476-5381.2012.01837.x.
Ref 4 Co-expression of Na(V) subunits alters the kinetics of inhibition of voltage-gated sodium channels by pore-blocking -conotoxins. Br J Pharmacol. 2013 Apr;168(7):1597-610. doi: 10.1111/bph.12051.
Ref 5 Structural basis for tetrodotoxin-resistant sodium channel binding by mu-conotoxin SmIIIA. J Biol Chem. 2003 Nov 21;278(47):46805-13. doi: 10.1074/jbc.M309222200. Epub 2003 Sep 10.
Ref 6 Pruning nature: Biodiversity-derived discovery of novel sodium channel blocking conotoxins from Conus bullatus. Toxicon. 2009 Jan;53(1):90-8. doi: 10.1016/j.toxicon.2008.10.017. Epub 2008 Nov 20.
Ref 7 Characterization of the Conus bullatus genome and its venom-duct transcriptome. BMC Genomics. 2011 Jan 25;12:60. doi: 10.1186/1471-2164-12-60.
Ref 8 - and -subunit composition of voltage-gated sodium channels investigated with -conotoxins and the recently discovered O-conotoxin GVIIJ. J Neurophysiol. 2015 Apr 1;113(7):2289-301. doi: 10.1152/jn.01004.2014. Epub 2015 Jan 28.
Ref 9 Mammalian neuronal sodium channel blocker -conotoxin BuIIIB has a structured N-terminus that influences potency. ACS Chem Biol. 2013;8(6):1344-51. doi: 10.1021/cb300674x. Epub 2013 Apr 16.
Ref 10 The Birth and Death of Toxins with Distinct Functions: A Case Study in the Sea Anemone Nematostella. Mol Biol Evol. 2019 Sep 1;36(9):2001-2012. doi: 10.1093/molbev/msz132.
Ref 11 AbeTx1 Is a Novel Sea Anemone Toxin with a Dual Mechanism of Action on Shaker-Type K? Channels Activation. Mar Drugs. 2018 Oct 1;16(10):360. doi: 10.3390/md16100360.
Ref 12 A novel strategy for the identification of toxinlike structures in spider venom. Proteins. 2005 Apr 1;59(1):131-40. doi: 10.1002/prot.20390.
Ref 13 Unique bell-shaped voltage-dependent modulation of Na+ channel gating by novel insect-selective toxins from the spider Agelena orientalis. J Biol Chem. 2010 Jun 11;285(24):18545-54. doi: 10.1074/jbc.M110.125211. Epub 2010 Apr 12.
Ref 14 Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II. J Biol Chem. 1989 Nov 15;264(32):19259-65.
Ref 15 The amino-acid sequence of neurotoxin II of Androctonus australis Hector. Eur J Biochem. 1972 Jul 24;28(3):381-8. doi: 10.1111/j.1432-1033.1972.tb01924.x.
Ref 16 Disulfide bonds of toxin II of the scorpion Androctonus australis Hector. Eur J Biochem. 1974 Sep 16;47(3):483-9. doi: 10.1111/j.1432-1033.1974.tb03716.x.
Ref 17 Characterization of Amm VIII from Androctonus mauretanicus mauretanicus: a new scorpion toxin that discriminates between neuronal and skeletal sodium channels. Biochem J. 2003 Nov 1;375(Pt 3):551-60. doi: 10.1042/BJ20030688.
Ref 18 Expression of the standard scorpion alpha-toxin AaH II and AaH II mutants leading to the identification of some key bioactive elements. Biochim Biophys Acta. 2005 May 25;1723(1-3):91-9. doi: 10.1016/j.bbagen.2005.01.008. Epub 2005 Jan 29.
Ref 19 The scorpion toxin Amm VIII induces pain hypersensitivity through gain-of-function of TTX-sensitive Na? channels. Pain. 2013 Aug;154(8):1204-15. doi: 10.1016/j.pain.2013.03.037. Epub 2013 Apr 6.
Ref 20 Orthorhombic crystals and three-dimensional structure of the potent toxin II from the scorpion Androctonus australis Hector. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7443-7. doi: 10.1073/pnas.85.20.7443.
Ref 21 Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 A resolution. J Mol Biol. 1994 Apr 22;238(1):88-103. doi: 10.1006/jmbi.1994.1270.
Ref 22 Ab initio structure determination and refinement of a scorpion protein toxin. Acta Crystallogr D Biol Crystallogr. 1997 Sep 1;53(Pt 5):551-7. doi: 10.1107/S0907444997005386.
Ref 23 Molecular basis of the high insecticidal potency of scorpion alpha-toxins. J Biol Chem. 2004 Jul 23;279(30):31679-86. doi: 10.1074/jbc.M402048200. Epub 2004 May 8.
Ref 24 Peptide ion channel toxins from the bootlace worm, the longest animal on Earth. Sci Rep. 2018 Mar 22;8(1):4596. doi: 10.1038/s41598-018-22305-w.
Ref 25 Functional Characterization of the Nemertide Family of Peptide Toxins. J Nat Prod. 2021 Aug 27;84(8):2121-2128. doi: 10.1021/acs.jnatprod.1c00104. Epub 2021 Aug 16.
Ref 26 Genomic characterisation of the toxin Amm VIII from the scorpion Androctonus mauretanicus mauretanicus. Toxicon. 2006 Apr;47(5):531-6. doi: 10.1016/j.toxicon.2006.01.005. Epub 2006 Mar 14.
Ref 27 New analysis of the toxic compounds from the Androctonus mauretanicus mauretanicus scorpion venom. Toxicon. 2008 Apr;51(5):835-52. doi: 10.1016/j.toxicon.2007.12.012. Epub 2007 Dec 17.
Ref 28 Involvement of endogenous opioid system in scorpion toxin-induced antinociception in mice. Neurosci Lett. 2010 Sep 20;482(1):45-50. doi: 10.1016/j.neulet.2010.06.090. Epub 2010 Jul 7.
Ref 29 A new sea anemone peptide, APETx2, inhibits ASIC3, a major acid-sensitive channel in sensory neurons. EMBO J. 2004 Apr 7;23(7):1516-25. doi: 10.1038/sj.emboj.7600177. Epub 2004 Mar 25.
Ref 30 ASIC3, a sensor of acidic and primary inflammatory pain. EMBO J. 2008 Nov 19;27(22):3047-55. doi: 10.1038/emboj.2008.213. Epub 2008 Oct 16.
Ref 31 Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon. 2009 Jul;54(1):56-61. doi: 10.1016/j.toxicon.2009.03.014. Epub 2009 Mar 21.
Ref 32 Expression in Pichia pastoris and characterization of APETx2, a specific inhibitor of acid sensing ion channel 3. Toxicon. 2010 Dec;56(8):1388-97. doi: 10.1016/j.toxicon.2010.08.004. Epub 2010 Sep 9.
Ref 33 Inhibition of voltage-gated Na(+) currents in sensory neurones by the sea anemone toxin APETx2. Br J Pharmacol. 2012 Apr;165(7):2167-77. doi: 10.1111/j.1476-5381.2011.01674.x.
Ref 34 A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins. FASEB J. 2012 Dec;26(12):5141-51. doi: 10.1096/fj.12-218479. Epub 2012 Sep 12.
Ref 35 Cyclisation increases the stability of the sea anemone peptide APETx2 but decreases its activity at acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1511-1527. doi: 10.3390/md10071511. Epub 2012 Jul 16.
Ref 36 Functional expression in Escherichia coli of the disulfide-rich sea anemone peptide APETx2, a potent blocker of acid-sensing ion channel 3. Mar Drugs. 2012 Jul;10(7):1605-1618. doi: 10.3390/md10071605. Epub 2012 Jul 23.
Ref 37 Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels. Protein Sci. 2005 Aug;14(8):2003-10. doi: 10.1110/ps.051378905. Epub 2005 Jun 29.
Ref 38 Understanding the molecular basis of toxin promiscuity: the analgesic sea anemone peptide APETx2 interacts with acid-sensing ion channel 3 and hERG channels via overlapping pharmacophores. J Med Chem. 2014 Nov 13;57(21):9195-203. doi: 10.1021/jm501400p. Epub 2014 Nov 4.
Ref 39 Compound Heterozygous SCN5A Mutations in Severe Sodium Channelopathy With Brugada Syndrome: A Case Report. Front Cardiovasc Med. 2020 Jul 24;7:117. doi: 10.3389/fcvm.2020.00117. eCollection 2020.
Ref 40 Cloning and characterization of the cDNA sequences of two venom peptides from Chinese scorpion Buthus martensii Karsch (BmK). Toxicon. 2000 Jul;38(7):893-9. doi: 10.1016/s0041-0101(99)00192-0.
Ref 41 Nine novel precursors of Buthus martensii scorpion alpha-toxin homologues. Toxicon. 2000 Dec;38(12):1653-61. doi: 10.1016/s0041-0101(00)00081-7.
Ref 42 Recombinant expression, purification, and characterization of scorpion toxin BmTX14. Protein Expr Purif. 2012 Apr;82(2):325-31. doi: 10.1016/j.pep.2012.02.001. Epub 2012 Feb 10.
Ref 43 Delta-conotoxin GmVIA, a novel peptide from the venom of Conus gloriamaris. Biochemistry. 1994 Sep 27;33(38):11420-5. doi: 10.1021/bi00204a003.
Ref 44 Alterations of voltage-activated sodium current by a novel conotoxin from the venom of Conus gloriamaris. J Neurophysiol. 1995 Mar;73(3):1295-301. doi: 10.1152/jn.1995.73.3.1295.
Ref 45 Distinction among neuronal subtypes of voltage-activated sodium channels by mu-conotoxin PIIIA. J Neurosci. 2000 Jan 1;20(1):76-80. doi: 10.1523/JNEUROSCI.20-01-00076.2000.
Ref 46 Purification, characterization, synthesis, and cloning of the lockjaw peptide from Conus purpurascens venom. Biochemistry. 1995 Apr 18;34(15):4913-8. doi: 10.1021/bi00015a002.
Ref 47 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 48 Delta-conotoxin structure/function through a cladistic analysis. Biochemistry. 2001 Nov 6;40(44):13201-8. doi: 10.1021/bi010683a.
Ref 49 Potency optimization of Huwentoxin-IV on hNav1.7: a neurotoxin TTX-S sodium-channel antagonist from the venom of the Chinese bird-eating spider Selenocosmia huwena. Peptides. 2013 Jun;44:40-6. doi: 10.1016/j.peptides.2013.03.011. Epub 2013 Mar 19.
Ref 50 Re-engineering the -conotoxin SIIIA scaffold. Biopolymers. 2014 Apr;101(4):347-54. doi: 10.1002/bip.22368.
Ref 51 Neuronally micro-conotoxins from Conus striatus utilize an alpha-helical motif to target mammalian sodium channels. J Biol Chem. 2008 Aug 1;283(31):21621-8. doi: 10.1074/jbc.M802852200. Epub 2008 Jun 3.
Ref 52 N- and C-terminal extensions of -conotoxins increase potency and selectivity for neuronal sodium channels. Biopolymers. 2012;98(2):161-5. doi: 10.1002/bip.22032. Epub 2012 Feb 10.
Ref 53 Isolation and structure-activity of mu-conotoxin TIIIA, a potent inhibitor of tetrodotoxin-sensitive voltage-gated sodium channels. Mol Pharmacol. 2007 Mar;71(3):676-85. doi: 10.1124/mol.106.028225. Epub 2006 Dec 1.
Ref 54 Diversity and evolution of conotoxins in Conus virgo, Conus eburneus, Conus imperialis and Conus marmoreus from the South China Sea. Toxicon. 2012 Nov;60(6):982-9. doi: 10.1016/j.toxicon.2012.06.011. Epub 2012 Jul 7.
Ref 55 New sodium channel-blocking conotoxins also affect calcium currents in Lymnaea neurons. Biochemistry. 1995 Apr 25;34(16):5364-71. doi: 10.1021/bi00016a007.
Ref 56 A new family of conotoxins that blocks voltage-gated sodium channels. J Biol Chem. 1995 Jul 14;270(28):16796-802. doi: 10.1074/jbc.270.28.16796.
Ref 57 MicroO-conotoxin MrVIA inhibits mammalian sodium channels, but not through site I. J Neurophysiol. 1996 Sep;76(3):1423-9. doi: 10.1152/jn.1996.76.3.1423.
Ref 58 The muO-conotoxin MrVIA inhibits voltage-gated sodium channels by associating with domain-3. FEBS Lett. 2006 Feb 20;580(5):1360-4. doi: 10.1016/j.febslet.2006.01.057. Epub 2006 Jan 26.
Ref 59 Definition of the M-conotoxin superfamily: characterization of novel peptides from molluscivorous Conus venoms. Biochemistry. 2005 Jun 7;44(22):8176-86. doi: 10.1021/bi047541b.
Ref 60 mu-Conotoxin PIIIA, a new peptide for discriminating among tetrodotoxin-sensitive Na channel subtypes. J Neurosci. 1998 Jun 15;18(12):4473-81. doi: 10.1523/JNEUROSCI.18-12-04473.1998.
Ref 61 Structurally diverse -conotoxin PIIIA isomers block sodium channel NaV 1.4. Angew Chem Int Ed Engl. 2012 Apr 23;51(17):4058-61. doi: 10.1002/anie.201107011. Epub 2012 Mar 12.
Ref 62 Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels. J Biol Chem. 2002 Jul 26;277(30):27247-55. doi: 10.1074/jbc.M201611200. Epub 2002 May 2.
Ref 63 Molecular diversity and evolution of cystine knot toxins of the tarantula Chilobrachys jingzhao. Cell Mol Life Sci. 2008 Aug;65(15):2431-44. doi: 10.1007/s00018-008-8135-x.
Ref 64 Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao. Proteomics. 2007 Jun;7(11):1892-907. doi: 10.1002/pmic.200600785.
Ref 65 Effects and mechanism of Chinese tarantula toxins on the Kv2.1 potassium channels. Biochem Biophys Res Commun. 2007 Jan 19;352(3):799-804. doi: 10.1016/j.bbrc.2006.11.086. Epub 2006 Nov 27.
Ref 66 Characterization of the excitatory mechanism induced by Jingzhaotoxin-I inhibiting sodium channel inactivation. Toxicon. 2007 Sep 15;50(4):507-17. doi: 10.1016/j.toxicon.2007.04.018. Epub 2007 May 3.
Ref 67 Molecular determinants for the tarantula toxin jingzhaotoxin-I interacting with potassium channel Kv2.1. Toxicon. 2013 Mar 1;63:129-36. doi: 10.1016/j.toxicon.2012.12.001. Epub 2012 Dec 13.
Ref 68 Molecular determinant for the tarantula toxin Jingzhaotoxin-I slowing the fast inactivation of voltage-gated sodium channels. Toxicon. 2016 Mar 1;111:13-21. doi: 10.1016/j.toxicon.2015.12.009. Epub 2015 Dec 23.
Ref 69 Sequence-specific assignment of 1H-NMR resonance and determination of the secondary structure of Jingzhaotoxin-I. Acta Biochim Biophys Sin (Shanghai). 2005 Aug;37(8):567-72. doi: 10.1111/j.1745-7270.2005.00078.x.
Ref 70 Jingzhaotoxin-I, a novel spider neurotoxin preferentially inhibiting cardiac sodium channel inactivation. J Biol Chem. 2005 Apr 1;280(13):12069-76. doi: 10.1074/jbc.M411651200. Epub 2004 Nov 17.
Ref 71 Where cone snails and spiders meet: design of small cyclic sodium-channel inhibitors. FASEB J. 2019 Mar;33(3):3693-3703. doi: 10.1096/fj.201801909R. Epub 2018 Dec 3.
Ref 72 muO-conotoxin MrVIB selectively blocks Nav1.8 sensory neuron specific sodium channels and chronic pain behavior without motor deficits. Proc Natl Acad Sci U S A. 2006 Nov 7;103(45):17030-5. doi: 10.1073/pnas.0601819103. Epub 2006 Oct 31.
Ref 73 NMR-based mapping of disulfide bridges in cysteine-rich peptides: application to the mu-conotoxin SxIIIA. J Am Chem Soc. 2008 Oct 29;130(43):14280-6. doi: 10.1021/ja804303p. Epub 2008 Oct 3.
Ref 74 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 75 Conus geographus toxins that discriminate between neuronal and muscle sodium channels. J Biol Chem. 1985 Aug 5;260(16):9280-8.
Ref 76 The amino acid sequences of homologous hydroxyproline-containing myotoxins from the marine snail Conus geographus venom. FEBS Lett. 1983 May 8;155(2):277-80. doi: 10.1016/0014-5793(82)80620-0.
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