Target Information

General Information of This Target
Target ID
BTDT00055
Target Name
Sodium channel protein type 4 subunit alpha (Scn4a)
Target Bioclass
Transporter and channel
Uniprot ID
P15390
3D Structure
Download
2D Sequence
3D Structure
Source
Predict by Alphafold2
?
Alphafold Parameters: msa_mode: mmseqs2_uniref_env model_type: auto num_recycles: auto
Gene Name
Scn4a
Gene ID
25722
Synonym
Mu-1; SkM1; Sodium channel protein skeletal muscle subunit alpha; Sodium channel protein type IV subunit alpha; Voltage-gated sodium channel subunit alpha Nav1.4
Sequence
MASSSLPNLVPPGPHCLRPFTPESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEA
GKNLPLIYGDPPPEVIGIPLEDLDPYYSDKKTFIVLNKGKAIFRFSATPALYLLSPFSIV
RRVAIKVLIHALFSMFIMITILTNCVFMTMSNPPSWSKHVEYTFTGIYTFESLIKMLARG
FCIDDFTFLRDPWNWLDFSVITMAYVTEFVDLGNISALRTFRVLRALKTITVIPGLKTIV
GALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPMNDTNTTWYGNDTW
YSNDTWYGNDTWYINDTWNSQESWAGNSTFDWEAYINDEGNFYFLEGSNDALLCGNSSDA
GHCPEGYECIKAGRNPNYGYTSYDTFSWAFLALFRLMTQDYWENLFQLTLRAAGKTYMIF
FVVIIFLGSFYLINLILAVVAMAYAEQNEATLAEDQEKEEEFQQMLEKYKKHQEELEKAK
AAQALESGEEADGDPTHNKDCNGSLDASGEKGPPRPSCSADSAISDAMEELEEAHQKCPP
WWYKCAHKVLIWNCCAPWVKFKHIIYLIVMDPFVDLGITICIVLNTLFMAMEHYPMTEHF
DNVLSVGNLVFTGIFTAEMVLKLIAMDPYEYFQQGWNIFDSFIVTLSLVELGLANVQGLS
VLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSY
KECVCKIASDCNLPRWHMNDFFHSFLIVFRILCGEWIETMWDCMEVAGQAMCLTVFLMVM
VIGNLVVLNLFLALLLSSFSADSLAASDEDGEMNNLQIAIGRIKWGIGFAKTFLLGLLRG
KILSPKEIILSLGEPGGAGENAEESTPEDEKKEPPPEDKELKDNHILNHVGLTDGPRSSI
ELDHLNFINNPYLTIQVPIASEESDLEMPTEEETDAFSEPEDIKKPLQPLYDGNSSVCST
ADYKPPEEDPEEQAEENPEGEQPEECFTEACVKRCPCLYVDISQGRGKMWWTLRRACFKI
VEHNWFETFIVFMILLSSGALAFEDIYIEQRRVIRTILEYADKVFTYIFILEMLLKWVAY
GFKVYFTNAWCWLDFLIVDVSIISLVANWLGYSELGPIKSLRTLRALRPLRALSRFEGMR
VVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYYCVNTTTSERFDISVVNNKS
ESESLMYTGQVRWMNVKVNYDNVGLGYLSLLQVATFKGWMDIMYAAVDSREKEEQPHYEV
NLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGKDIFMTEEQKKYYNAMKKLG
SKKPQKPIPRPQNKIQGMVYDFVTKQVFDISIMILICLNMVTMMVETDDQSQLKVDILYN
INMVFIIIFTGECVLKMFALRHYYFTIGWNIFDFVVVILSIVGLALSDLIQKYFVSPTLF
RVIRLARIGRVLRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMSNFAYV
KKESGIDDMFNFETFGNSIICLFEITTSAGWDGLLNPILNSGPPDCDPTLENPGTNVRGD
CGNPSIGICFFCSYIIISFLIVVNMYIAIILENFNVATEESSEPLSEDDFEMFYETWEKF
DPDATQFIDYSRLSDFVDTLQEPLKIAKPNKIKLITLDLPMVPGDKIHCLDILFALTKEV
LGDSGEMDALKQTMEEKFMAANPSKVSYEPITTTLKRKQEEVCAIKIQRAYRRHLLQRSV
KQASYMYRHSQDGNDDGAPEKEGLLANTMNKMYGHEKEGDGVQSQGEEEKASTEDAGPTV
EPEPTSSSDTALTPSPPPLPPSSSPPQGQTVRPGVKESLV

    Click to Show/Hide
Family
the sodium channel (TC 1.A.1.10) family
Function
Pore-forming subunit of a voltage-gated sodium channel complex through which Na(+) ions pass in accordance with their electrochemical gradient. Alternates between resting, activated and inactivated states. Required for normal muscle fiber excitability, normal muscle contraction and relaxation cycles, and constant muscle strength in the presence of fluctuating K(+) levels.

    Click to Show/Hide
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
0.22 nM
 [1- 5]
 Toxin Info    Mu-conotoxin BuIIIB Dissociation constant
0.34 - 3.6 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    Potassium channel toxin alpha-KTx 21.1 Inhibition rate . [12- 16]
 Toxin Info    Mu-hexatoxin-Mg2a Inhibition rate
23 %
 [17], [18]
 Toxin Info    Mu-hexatoxin-Mg2a Inhibition rate
35 %
 [17], [18]
 Toxin Info    Alpha-mammal toxin AaH2 Effective concentration 50
2.2 nM
 [19- 28]
 Toxin Info    Nemertide alpha-5 Effective concentration 50
9.4 nM
 [29], [30]
 Toxin Info    Nemertide alpha-4 Effective concentration 50
12.9 nM
 [29], [30]
 Toxin Info    Nemertide alpha-6 Effective concentration 50
105.6 nM
 [29], [30]
 Toxin Info    Nemertide alpha-2 Effective concentration 50
127.7 nM
 [29], [30]
 Toxin Info    Nemertide alpha-3 Effective concentration 50
138.9 nM
 [29], [30]
 Toxin Info    Nemertide alpha-3 Effective concentration 50
138.9 nM
 [29], [30]
 Toxin Info    Nemertide alpha-1 Effective concentration 50
145.5 nM
 [29], [30], [31]
 Toxin Info    Nemertide alpha-1 Effective concentration 50
145.5 nM
 [29], [30], [31]
 Toxin Info    Nemertide alpha-7 Effective concentration 50
170.2 nM
 [29], [30]
 Toxin Info    Alpha-toxin Amm8 Effective concentration 50
416 nM
 [22- 34]
 Toxin Info    Nemertide alpha-2 Effective concentration 50
1.1503 μM
 [29], [30]
 Toxin Info    Delta-conotoxin GmVIA Effective concentration 50
4.8 μM
 [35], [36], [37]
 Toxin Info    Delta-conotoxin PVIA Effective concentration 50
5.2 μM
 [38], [39], [37], [40]
 Toxin Info    Mu-conotoxin CnIIIC IC50
1.3 nM
 [3- 42]
 Toxin Info    Mu-conotoxin SIIIB IC50
3 nM
 [43], [44]
 Toxin Info    Mu-conotoxin SxIIIA IC50
7 nM
 [2- 45]
 Toxin Info    Mu-conotoxin SIIIC IC50
9 nM
 [46]
 Toxin Info    Mu-conotoxin TIIIA IC50
9 nM
 [2- 46]
 Toxin Info    Mu-conotoxin GIIIA IC50
19 - 110 nM
 [2- 58]
 Toxin Info    Mu-conotoxin PIIIA IC50
36 - 41 nM
 [2- 61]
 Toxin Info    Delta-theraphotoxin-Cg1a 2 IC50
339 nM
 [62- 68]
 Toxin Info    Delta-theraphotoxin-Cg1a 3 IC50
339 nM
 [62- 68]
 Toxin Info    Delta-theraphotoxin-Cg1a 1 IC50
339 nM
 [63- 69]
 Toxin Info    Mu-conotoxin MrVIA IC50
438 nM
 [37- 74]
 Toxin Info    HWTX-IV IC50
>10 μM
 [75]
 Toxin Info    PnM9 IC50
0.3 ± 0.1 μM
 [76]
 Toxin Info    PnCS2 IC50
0.6 ± 0.2 μM
 [76]
 Toxin Info    PnCS4 IC50
0.9 ± 0.2 μM
 [76]
 Toxin Info    PnM8 IC50
2.4 ± 0.1 μM
 [76]
 Toxin Info    PnM7 IC50
3.1 ± 0.2 μM
 [76]
 Toxin Info    Huwentoxin-IV IC50
3.9 - >10 μM
 [75- 92]
 Toxin Info    PnM5 IC50
8.3 ± 0.8 μM
 [76]
 Toxin Info    PnCS3 IC50
10.7 ± 0.7 μM
 [76]
 Toxin Info    PnCS2 IC50
14.3 ± 1.4 μM
 [76]
 Toxin Info    PnM6 IC50
32.4 ± 0.6 μM
 [76]
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 Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions. PLoS One. 2018 Mar 21;13(3):e0193739. doi: 10.1371/journal.pone.0193739. eCollection 2018.
Ref 13 Novel components of Tityus serrulatus venom: A transcriptomic approach. Toxicon. 2021 Jan 15;189:91-104. doi: 10.1016/j.toxicon.2020.11.001. Epub 2020 Nov 10.
Ref 14 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 15 Moving pieces in a venomic puzzle: unveiling post-translationally modified toxins from Tityus serrulatus. J Proteome Res. 2013 Jul 5;12(7):3460-70. doi: 10.1021/pr4003068. Epub 2013 Jun 13.
Ref 16 Influence of post-starvation extraction time and prey-specific diet in Tityus serrulatus scorpion venom composition and hyaluronidase activity. Toxicon. 2014 Nov;90:326-36. doi: 10.1016/j.toxicon.2014.08.064. Epub 2014 Sep 6.
Ref 17 Distinct primary structures of the major peptide toxins from the venom of the spider Macrothele gigas that bind to sites 3 and 4 in the sodium channel. FEBS Lett. 2003 Jul 17;547(1-3):43-50. doi: 10.1016/s0014-5793(03)00666-5.
Ref 18 Successful refolding and NMR structure of rMagi3: A disulfide-rich insecticidal spider toxin. Protein Sci. 2018 Mar;27(3):692-701. doi: 10.1002/pro.3363. Epub 2018 Jan 3.
Ref 19 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 20 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 21 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 22 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 23 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 24 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 25 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 26 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 27 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 28 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 29 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 30 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 31 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 32 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 33 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 34 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 35 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 36 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 37 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 38 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 39 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 40 Delta-conotoxin structure/function through a cladistic analysis. Biochemistry. 2001 Nov 6;40(44):13201-8. doi: 10.1021/bi010683a.
Ref 41 Large-scale discovery of conopeptides and conoproteins in the injectable venom of a fish-hunting cone snail using a combined proteomic and transcriptomic approach. J Proteomics. 2012 Sep 18;75(17):5215-25. doi: 10.1016/j.jprot.2012.06.001. Epub 2012 Jun 13.
Ref 42 Peptide therapeutics from venom: Current status and potential. Bioorg Med Chem. 2018 Jun 1;26(10):2738-2758. doi: 10.1016/j.bmc.2017.09.029. Epub 2017 Sep 23.
Ref 43 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 44 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 45 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 46 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 47 Evolution of separate predation- and defence-evoked venoms in carnivorous cone snails. Nat Commun. 2014 Mar 24;5:3521. doi: 10.1038/ncomms4521.
Ref 48 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 49 Conus geographus toxins that discriminate between neuronal and muscle sodium channels. J Biol Chem. 1985 Aug 5;260(16):9280-8.
Ref 50 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.
Ref 51 Disulfide pairings in geographutoxin I, a peptide neurotoxin from Conus geographus. FEBS Lett. 1990 May 7;264(1):29-32. doi: 10.1016/0014-5793(90)80756-9.
Ref 52 Active site of mu-conotoxin GIIIA, a peptide blocker of muscle sodium channels. J Biol Chem. 1991 Sep 15;266(26):16989-91.
Ref 53 Action of derivatives of mu-conotoxin GIIIA on sodium channels. Single amino acid substitutions in the toxin separately affect association and dissociation rates. Biochemistry. 1992 Sep 8;31(35):8229-38. doi: 10.1021/bi00150a016.
Ref 54 Role of hydroxyprolines in the in vitro oxidative folding and biological activity of conotoxins. Biochemistry. 2008 Feb 12;47(6):1741-51. doi: 10.1021/bi701934m. Epub 2008 Jan 12.
Ref 55 NMR Structure of -Conotoxin GIIIC: Leucine 18 Induces Local Repacking of the N-Terminus Resulting in Reduced Na(V) Channel Potency. Molecules. 2018 Oct 22;23(10):2715. doi: 10.3390/molecules23102715.
Ref 56 Solution structure of mu-conotoxin GIIIA analysed by 2D-NMR and distance geometry calculations. FEBS Lett. 1991 Jan 28;278(2):160-6. doi: 10.1016/0014-5793(91)80107-e.
Ref 57 Tertiary structure of conotoxin GIIIA in aqueous solution. Biochemistry. 1991 Jul 16;30(28):6908-16. doi: 10.1021/bi00242a014.
Ref 58 Structure-activity relationships of mu-conotoxin GIIIA: structure determination of active and inactive sodium channel blocker peptides by NMR and simulated annealing calculations. Biochemistry. 1992 Dec 22;31(50):12577-84. doi: 10.1021/bi00165a006.
Ref 59 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 60 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 61 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 62 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 63 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 64 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 65 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 66 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 67 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 68 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 69 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 70 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 71 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 72 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 73 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 74 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 75 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 76 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 77 cDNA sequence analysis of seven peptide toxins from the spider Selenocosmia huwena. Toxicon. 2003 Dec;42(7):715-23. doi: 10.1016/j.toxicon.2003.08.007.
Ref 78 Molecular diversification based on analysis of expressed sequence tags from the venom glands of the Chinese bird spider Ornithoctonus huwena. Toxicon. 2008 Jun 15;51(8):1479-89. doi: 10.1016/j.toxicon.2008.03.024. Epub 2008 Mar 27.
Ref 79 Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. J Biol Chem. 2002 Dec 6;277(49):47564-71. doi: 10.1074/jbc.M204063200. Epub 2002 Sep 11.
Ref 80 Native pyroglutamation of huwentoxin-IV: a post-translational modification that increases the trapping ability to the sodium channel. PLoS One. 2013 Jun 24;8(6):e65984. doi: 10.1371/journal.pone.0065984. Print 2013.
Ref 81 Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain ii voltage sensor in the closed configuration. J Biol Chem. 2008 Oct 3;283(40):27300-13. doi: 10.1074/jbc.M708447200. Epub 2008 Jul 14.
Ref 82 Synthesis and characterization of huwentoxin-IV, a neurotoxin inhibiting central neuronal sodium channels. Toxicon. 2008 Feb;51(2):230-9. doi: 10.1016/j.toxicon.2007.09.008. Epub 2007 Sep 29.
Ref 83 The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation. Mol Pharmacol. 2010 Dec;78(6):1124-34. doi: 10.1124/mol.110.066332. Epub 2010 Sep 20.
Ref 84 Common molecular determinants of tarantula huwentoxin-IV inhibition of Na+ channel voltage sensors in domains II and IV. J Biol Chem. 2011 Aug 5;286(31):27301-10. doi: 10.1074/jbc.M111.246876. Epub 2011 Jun 9.
Ref 85 Engineering potent and selective analogues of GpTx-1, a tarantula venom peptide antagonist of the Na(V)1.7 sodium channel. J Med Chem. 2015 Mar 12;58(5):2299-314. doi: 10.1021/jm501765v. Epub 2015 Feb 19.
Ref 86 Gating modifier toxins isolated from spider venom: Modulation of voltage-gated sodium channels and the role of lipid membranes. J Biol Chem. 2018 Jun 8;293(23):9041-9052. doi: 10.1074/jbc.RA118.002553. Epub 2018 Apr 27.
Ref 87 Screening, large-scale production and structure-based classification of cystine-dense peptides. Nat Struct Mol Biol. 2018 Mar;25(3):270-278. doi: 10.1038/s41594-018-0033-9. Epub 2018 Feb 26.
Ref 88 Chemical Synthesis, Proper Folding, Na(v) Channel Selectivity Profile and Analgesic Properties of the Spider Peptide Phlotoxin 1. Toxins (Basel). 2019 Jun 21;11(6):367. doi: 10.3390/toxins11060367.
Ref 89 Analysis of the structural and molecular basis of voltage-sensitive sodium channel inhibition by the spider toxin huwentoxin-IV (-TRTX-Hh2a). J Biol Chem. 2013 Aug 2;288(31):22707-20. doi: 10.1074/jbc.M113.461392. Epub 2013 Jun 12.
Ref 90 Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNa(V)1.7. Biochim Biophys Acta Biomembr. 2017 May;1859(5):835-844. doi: 10.1016/j.bbamem.2017.01.020. Epub 2017 Jan 20.
Ref 91 The structure, dynamics and selectivity profile of a NaV1.7 potency-optimised huwentoxin-IV variant. PLoS One. 2017 Mar 16;12(3):e0173551. doi: 10.1371/journal.pone.0173551. eCollection 2017.
Ref 92 Structures of human Na(v)1.7 channel in complex with auxiliary subunits and animal toxins. Science. 2019 Mar 22;363(6433):1303-1308. doi: 10.1126/science.aaw2493. Epub 2019 Feb 14.
Data Quality & Feedback

Help us maintain data quality by reporting any errors or inaccuracies you may find.

samedaypayday.com visits since 2024

If you find any error in data or bug in web service, please kindly report it to biodb_contact@163.com et al.