General Information of This Target
Target ID
BTDT00139
Target Name
Potassium voltage-gated channel subfamily B member 1 (KCNB1)
Target Bioclass
Transporter and channel
Uniprot ID
Q14721
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
KCNB1
Gene ID
3745
Synonym
Delayed rectifier potassium channel 1; Voltage-gated potassium channel subunit Kv2.1
Sequence
MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKL
RDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELD
YWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLE
KPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWF
TMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFR
IMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTK
FKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFY
KEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFARSIEMMDIVVEKNGENMGKKDKVQD
NHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQ
SQPILNTKESAAQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPE
ATRFSHSPLTSLPSKTGGSTAPEVGWRGALGASGGRFVEANPSPDASQHSSFFIESPKSS
MKTNNPLKLRALKVNFMEGDPSPLLPVLGMYHDPLRNRGSAAAAVAGLECATLLDKAVLS
PESSIYTTASAKTPPRSPEKHTAIAFNFEAGVHQYIDADTDDEGQLLYSVDSSPPKSLPG
STSPKFSTGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKGPSGQEKCKLENHISPD
VRVLPGGGAHGSTRDQSI

    Click to Show/Hide
Family
the potassium channel family
Function
Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Plays also a role in the regulation of exocytosis independently of its electrical function. Forms tetrameric potassium- selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes. Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic- treated pulmonary artery smooth muscle cells. Channel properties are also modulated by cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the slowly inactivating delayed- rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle cells. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus. Contributes to the regulation of glucose-induced action potential amplitude and duration in pancreatic beta cells, hence limiting calcium influx and insulin secretion. Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits. Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner.

    Click to Show/Hide
Taxonomy ID
9606
TCDB ID
1.A.1.2.11
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Primates
Family: Hominidae
Genus: Homo
Species: Homo sapiens
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    GxTx1E (S13C,K27[Pra],M35[Nle]) Dissociation constant
0.83 nM
[1]
 Toxin Info    Kappa-theraphotoxin-Pg1a Dissociation constant
5.1 nM
[2], [3], [4], [5]
 Toxin Info    GxTx1E (S13C,M35[Nle]) Dissociation constant
26.9 nM
[6]
 Toxin Info    Kappa-theraphotoxin-Gr1a Dissociation constant
102 nM
[3- 12]
 Toxin Info    Toxin LmKTx2 Dissociation constant
125 nM
[13]
 Toxin Info    GxTx1E (M35[Nle]) Dissociation constant
224 nM
[13]
 Toxin Info    GxTx1E (M35[Nle],P36A) Dissociation constant
250 nM
[13]
 Toxin Info    GxTx1E (M35A) Dissociation constant
306 nM
[13]
 Toxin Info    GxTx1E (P34A,M35[Nle]) Dissociation constant
348 nM
[13]
 Toxin Info    GxTx1E (G6A,M35[Nle]) Dissociation constant
379 nM
[13]
 Toxin Info    GxTx1E (E1A,M35[Nle]) Dissociation constant
414 nM
[13]
 Toxin Info    GxTx1E (K21A,M35[Nle]) Dissociation constant
440 nM
[13]
 Toxin Info    GxTx1E (G14A,M35[Nle]) Dissociation constant
461 nM
[13]
 Toxin Info    GxTx1E (F33A,M35[Nle]) Dissociation constant
491 nM
[13]
 Toxin Info    GxTx1E (V23A,M35[Nle]) Dissociation constant
516 nM
[13]
 Toxin Info    GxTx1E (S13A,M35[Nle]) Dissociation constant
545 nM
[13]
 Toxin Info    GxTx1E (P20A,M35[Nle]) Dissociation constant
652 nM
[13]
 Toxin Info    GxTx1E (K27A,M35[Nle]) Dissociation constant
763 nM
[13]
 Toxin Info    GxTx1E (P26A,M35[Nle]) Dissociation constant
813 nM
[13]
 Toxin Info    GxTx1E (N32A,M35[Nle]) Dissociation constant
1.228 μM
[13]
 Toxin Info    GxTx1E (L30A,M35[Nle]) Dissociation constant
2.474 μM
[13]
 Toxin Info    GxTx1E (W9A,M35[Nle]) Dissociation constant
5.837 μM
[13]
 Toxin Info    GxTx1E (W8A,M35[Nle]) Dissociation constant
9.641 μM
[13]
 Toxin Info    GxTx1E (G5A,M35[Nle]) Dissociation constant
13.652 μM
[13]
 Toxin Info    Omega-theraphotoxin-Gr1a Dissociation constant
19 μM
[10- 18]
 Toxin Info    GxTx1E (G12A,M35[Nle]) Dissociation constant
21.755 μM
[13]
 Toxin Info    GxTx1E (P16A,M35[Nle]) Dissociation constant
22.967 μM
[13]
 Toxin Info    GxTx1E (Y22A,M35[Nle]) Dissociation constant
35.337 μM
[13]
 Toxin Info    GxTx1E (F7A,M35[Nle]) Dissociation constant
89.033 μM
[13]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Inhibition rate . [19]
 Toxin Info    Jingzhaotoxin F7-15.33 Inhibition rate . [20]
 Toxin Info    Apamin Inhibition rate . [21- 38]
 Toxin Info    Kappa-stichotoxin-She3a Inhibition rate . [39]
 Toxin Info    Mu-theraphotoxin-Cg1a Inhibition rate . [40], [41], [42], [43]
 Toxin Info    U-actitoxin-Oulsp1 Inhibition rate . [44]
 Toxin Info    Potassium channel toxin gamma-KTx 1.1 Inhibition rate . [45- 56]
 Toxin Info    Beta/omega-theraphotoxin-Tp2a Inhibition rate
5 %
[57- 76]
 Toxin Info    Pi-stichotoxin-Hcr5b Inhibition rate
33 %
[77]
 Toxin Info    Kappa-actitoxin-Ael2e Inhibition rate
39 %
[78]
 Toxin Info    Beta/omega-theraphotoxin-Tp1a Inhibition rate
60 %
[57- 82]
 Toxin Info    Kappa-theraphotoxin-Pg1b IC50
1.7 nM
[2]
 Toxin Info    Beta/omega-theraphotoxin-Tp1a IC50
411 nM
[57- 82]
 Toxin Info    Delta/kappa-theraphotoxin-Pm1a IC50
430 nM
[83]
 Toxin Info    VsTx1 IC50
1.22 μM
[84]
 Toxin Info    U20-theraphotoxin-Cg1a 1 IC50
3.62 μM
[85]
References
Ref 1 Distinguishing Potassium Channel Resting State Conformations in Live Cells with Environment-Sensitive Fluorescence. ACS Chem Neurosci. 2020 Aug 5;11(15):2316-2326. doi: 10.1021/acschemneuro.0c00276. Epub 2020 Jul 9.
Ref 2 Blockers of the delayed-rectifier potassium current in pancreatic beta-cells enhance glucose-dependent insulin secretion. Diabetes. 2006 Apr;55(4):1034-42. doi: 10.2337/diabetes.55.04.06.db05-0788.
Ref 3 Gating modifier peptides as probes of pancreatic beta-cell physiology. Toxicon. 2007 Feb;49(2):231-8. doi: 10.1016/j.toxicon.2006.09.012. Epub 2006 Sep 23.
Ref 4 A KV2.1 gating modifier binding assay suitable for high throughput screening. Channels (Austin). 2009 Nov;3(6):437-47. doi: 10.4161/chan.3.6.10201.
Ref 5 Solution structure of GxTX-1E, a high-affinity tarantula toxin interacting with voltage sensors in Kv2.1 potassium channels. Biochemistry. 2010 Jun 29;49(25):5134-42. doi: 10.1021/bi100246u.
Ref 6 Chemoselective tarantula toxins report voltage activation of wild-type ion channels in live cells. Proc Natl Acad Sci U S A. 2014 Nov 4;111(44):E4789-96. doi: 10.1073/pnas.1406876111. Epub 2014 Oct 20.
Ref 7 An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron. 1995 Oct;15(4):941-9. doi: 10.1016/0896-6273(95)90184-1.
Ref 8 Hanatoxin modifies the gating of a voltage-dependent K+ channel through multiple binding sites. Neuron. 1997 Apr;18(4):665-73. doi: 10.1016/s0896-6273(00)80306-2.
Ref 9 Mapping the receptor site for hanatoxin, a gating modifier of voltage-dependent K+ channels. Neuron. 1997 Apr;18(4):675-82. doi: 10.1016/s0896-6273(00)80307-4.
Ref 10 Gating modifier toxins reveal a conserved structural motif in voltage-gated Ca2+ and K+ channels. Proc Natl Acad Sci U S A. 1998 Jul 21;95(15):8585-9. doi: 10.1073/pnas.95.15.8585.
Ref 11 Voltage-sensor activation with a tarantula toxin as cargo. Nature. 2005 Aug 11;436(7052):857-60. doi: 10.1038/nature03873.
Ref 12 Solution structure of hanatoxin1, a gating modifier of voltage-dependent K(+) channels: common surface features of gating modifier toxins. J Mol Biol. 2000 Mar 31;297(3):771-80. doi: 10.1006/jmbi.2000.3609.
Ref 13 Tarantula toxins use common surfaces for interacting with Kv and ASIC ion channels. Elife. 2015 May 7;4:e06774. doi: 10.7554/eLife.06774.
Ref 14 Characterization of voltage-dependent calcium channel blocking peptides from the venom of the tarantula Grammostola rosea. Toxicon. 2011 Sep 1;58(3):265-76. doi: 10.1016/j.toxicon.2011.06.006. Epub 2011 Jun 28.
Ref 15 Complete and reversible block by omega-grammotoxin SIA of glutamatergic synaptic transmission between cultured rat hippocampal neurons. Neurosci Lett. 1995 Dec 8;201(2):135-8. doi: 10.1016/0304-3940(95)12169-2.
Ref 16 Voltage-dependent inhibition of N- and P-type calcium channels by the peptide toxin omega-grammotoxin-SIA. Mol Pharmacol. 1997 Dec;52(6):1095-104. doi: 10.1124/mol.52.6.1095.
Ref 17 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 18 Solution structure of omega-grammotoxin SIA, a gating modifier of P/Q and N-type Ca(2+) channel. J Mol Biol. 2002 Aug 16;321(3):517-26. doi: 10.1016/s0022-2836(02)00595-8.
Ref 19 Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005 Apr;67(4):1369-81. doi: 10.1124/mol.104.008193. Epub 2005 Jan 21.
Ref 20 Jingzhaotoxin-X, a gating modifier of Kv4.2 and Kv4.3 potassium channels purified from the venom of the Chinese tarantula Chilobrachys jingzhao. J Venom Anim Toxins Incl Trop Dis. 2020 May 29;26:e20190043. doi: 10.1590/1678-9199-JVATITD-2019-0043.
Ref 21 The precursors of the bee venom constituents apamin and MCD peptide are encoded by two genes in tandem which share the same 3'-exon. J Biol Chem. 1995 May 26;270(21):12704-8. doi: 10.1074/jbc.270.21.12704.
Ref 22 The peptide components of bee venom. Eur J Biochem. 1976 Jan 15;61(2):369-76. doi: 10.1111/j.1432-1033.1976.tb10030.x.
Ref 23 Apamin as a selective blocker of the calcium-dependent potassium channel in neuroblastoma cells: voltage-clamp and biochemical characterization of the toxin receptor. Proc Natl Acad Sci U S A. 1982 Feb;79(4):1308-12. doi: 10.1073/pnas.79.4.1308.
Ref 24 Apamin, a blocker of the calcium-activated potassium channel, induces neurodegeneration of Purkinje cells exclusively. Brain Res. 1997 Dec 19;778(2):405-8. doi: 10.1016/s0006-8993(97)01165-7.
Ref 25 Determinants of apamin and d-tubocurarine block in SK potassium channels. J Biol Chem. 1997 Sep 12;272(37):23195-200. doi: 10.1074/jbc.272.37.23195.
Ref 26 Pharmacological characterization of small-conductance Ca(2+)-activated K(+) channels stably expressed in HEK 293 cells. Br J Pharmacol. 2000 Mar;129(5):991-9. doi: 10.1038/sj.bjp.0703120.
Ref 27 SK3 is an important component of K(+) channels mediating the afterhyperpolarization in cultured rat SCG neurones. J Physiol. 2001 Sep 1;535(Pt 2):323-34. doi: 10.1111/j.1469-7793.2001.00323.x.
Ref 28 Apamin interacts with all subtypes of cloned small-conductance Ca2+-activated K+ channels. Pflugers Arch. 2001 Jan;441(4):544-50. doi: 10.1007/s004240000447.
Ref 29 An amino acid outside the pore region influences apamin sensitivity in small conductance Ca2+-activated K+ channels. J Biol Chem. 2007 Feb 9;282(6):3478-86. doi: 10.1074/jbc.M607213200. Epub 2006 Dec 1.
Ref 30 Apamin reduces neuromuscular transmission by activating inhibitory muscarinic M(2) receptors on motor nerve terminals. Eur J Pharmacol. 2010 Jan 25;626(2-3):239-43. doi: 10.1016/j.ejphar.2009.09.064. Epub 2009 Oct 8.
Ref 31 Allosteric block of KCa2 channels by apamin. J Biol Chem. 2010 Aug 27;285(35):27067-27077. doi: 10.1074/jbc.M110.110072. Epub 2010 Jun 18.
Ref 32 The small neurotoxin apamin blocks not only small conductance Ca(2+) activated K(+) channels (SK type) but also the voltage dependent Kv1.3 channel. Eur Biophys J. 2017 Sep;46(6):517-523. doi: 10.1007/s00249-016-1196-0. Epub 2017 Jan 20.
Ref 33 Apamin inhibits TNF-- and IFN--induced inflammatory cytokines and chemokines via suppressions of NF-B signaling pathway and STAT in human keratinocytes. Pharmacol Rep. 2017 Oct;69(5):1030-1035. doi: 10.1016/j.pharep.2017.04.006. Epub 2017 Apr 18.
Ref 34 Apamin Suppresses LPS-Induced Neuroinflammatory Responses by Regulating SK Channels and TLR4-Mediated Signaling Pathways. Int J Mol Sci. 2020 Jun 17;21(12):4319. doi: 10.3390/ijms21124319.
Ref 35 Apamin from bee venom suppresses inflammation in a murine model of gouty arthritis. J Ethnopharmacol. 2020 Jul 15;257:112860. doi: 10.1016/j.jep.2020.112860. Epub 2020 Apr 11.
Ref 36 Antioxidative, Antiapoptotic, and Anti-Inflammatory Effects of Apamin in a Murine Model of Lipopolysaccharide-Induced Acute Kidney Injury. Molecules. 2020 Dec 3;25(23):5717. doi: 10.3390/molecules25235717.
Ref 37 Solution structure of apamin determined by nuclear magnetic resonance and distance geometry. Biochemistry. 1988 Nov 1;27(22):8491-8. doi: 10.1021/bi00422a029.
Ref 38 Binding and toxicity of apamin. Characterization of the active site. Eur J Biochem. 1991 Mar 28;196(3):639-45. doi: 10.1111/j.1432-1033.1991.tb15860.x.
Ref 39 Stichodactyla helianthus peptide, a pharmacological tool for studying Kv3.2 channels. Mol Pharmacol. 2005 May;67(5):1513-21. doi: 10.1124/mol.105.011064. Epub 2005 Feb 11.
Ref 40 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 41 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 42 Expression and characterization of jingzhaotoxin-34, a novel neurotoxin from the venom of the tarantula Chilobrachys jingzhao. Peptides. 2009 Jun;30(6):1042-8. doi: 10.1016/j.peptides.2009.02.018. Epub 2009 Mar 13.
Ref 43 Selective Closed-State Nav1.7 Blocker JZTX-34 Exhibits Analgesic Effects against Pain. Toxins (Basel). 2018 Feb 2;10(2):64. doi: 10.3390/toxins10020064.
Ref 44 Structure, folding and stability of a minimal homologue from Anemonia sulcata of the sea anemone potassium channel blocker ShK. Peptides. 2018 Jan;99:169-178. doi: 10.1016/j.peptides.2017.10.001. Epub 2017 Oct 6.
Ref 45 A large number of novel Ergtoxin-like genes and ERG K+-channels blocking peptides from scorpions of the genus Centruroides. FEBS Lett. 2002 Dec 4;532(1-2):121-6. doi: 10.1016/s0014-5793(02)03652-9.
Ref 46 A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom. FASEB J. 1999 May;13(8):953-62.
Ref 47 Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel. FEBS Lett. 2000 Aug 18;479(3):156-7. doi: 10.1016/s0014-5793(00)01891-3.
Ref 48 Mapping the receptor site for ergtoxin, a specific blocker of ERG channels. FEBS Lett. 2002 Jan 2;510(1-2):45-9. doi: 10.1016/s0014-5793(01)03218-5.
Ref 49 Mapping the binding site of a human ether-a-go-go-related gene-specific peptide toxin (ErgTx) to the channel's outer vestibule. J Biol Chem. 2002 May 10;277(19):16403-11. doi: 10.1074/jbc.M200460200. Epub 2002 Feb 25.
Ref 50 Preferential closed channel blockade of HERG potassium currents by chemically synthesised BeKm-1 scorpion toxin. FEBS Lett. 2003 Jul 17;547(1-3):20-6. doi: 10.1016/s0014-5793(03)00662-8.
Ref 51 Species diversity and peptide toxins blocking selectivity of ether-a-go-go-related gene subfamily K+ channels in the central nervous system. Mol Pharmacol. 2006 May;69(5):1673-83. doi: 10.1124/mol.105.019729. Epub 2006 Feb 23.
Ref 52 Mechanism of block of the hERG K+ channel by the scorpion toxin CnErg1. Biophys J. 2007 Jun 1;92(11):3915-29. doi: 10.1529/biophysj.106.101956. Epub 2007 Mar 16.
Ref 53 Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function. Peptides. 2011 Mar;32(3):560-7. doi: 10.1016/j.peptides.2010.06.018. Epub 2010 Jun 30.
Ref 54 Positive selection-guided mutational analysis revealing two key functional sites of scorpion ERG K(+) channel toxins. Biochem Biophys Res Commun. 2012 Dec 7;429(1-2):111-6. doi: 10.1016/j.bbrc.2012.10.065. Epub 2012 Oct 24.
Ref 55 Solution structure of CnErg1 (Ergtoxin), a HERG specific scorpion toxin. FEBS Lett. 2003 Mar 27;539(1-3):138-42. doi: 10.1016/s0014-5793(03)00216-3.
Ref 56 Exploring structural features of the interaction between the scorpion toxinCnErg1 and ERG K+ channels. Proteins. 2004 Aug 1;56(2):367-75. doi: 10.1002/prot.20102.
Ref 57 Two tarantula peptides inhibit activation of multiple sodium channels. Biochemistry. 2002 Dec 17;41(50):14734-47. doi: 10.1021/bi026546a.
Ref 58 Differential phospholipid binding by site 3 and site 4 toxins. Implications for structural variability between voltage-sensitive sodium channel domains. J Biol Chem. 2005 Mar 25;280(12):11127-33. doi: 10.1074/jbc.M412552200. Epub 2005 Jan 4.
Ref 59 Molecular interactions of the gating modifier toxin ProTx-II with NaV 1.5: implied existence of a novel toxin binding site coupled to activation. J Biol Chem. 2007 Apr 27;282(17):12687-97. doi: 10.1074/jbc.M610462200. Epub 2007 Mar 5.
Ref 60 ProTx-I and ProTx-II: gating modifiers of voltage-gated sodium channels. Toxicon. 2007 Feb;49(2):194-201. doi: 10.1016/j.toxicon.2006.09.014. Epub 2006 Sep 27.
Ref 61 Inhibition of sodium channel gating by trapping the domain II voltage sensor with protoxin II. Mol Pharmacol. 2008 Mar;73(3):1020-8. doi: 10.1124/mol.107.041046. Epub 2007 Dec 21.
Ref 62 ProTx-II, a selective inhibitor of NaV1.7 sodium channels, blocks action potential propagation in nociceptors. Mol Pharmacol. 2008 Nov;74(5):1476-84. doi: 10.1124/mol.108.047670. Epub 2008 Aug 26.
Ref 63 Evidence for multiple effects of ProTxII on activation gating in Na(V)1.5. Toxicon. 2008 Sep 1;52(3):489-500. doi: 10.1016/j.toxicon.2008.06.023. Epub 2008 Jul 9.
Ref 64 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 65 Inhibition of the activation pathway of the T-type calcium channel Ca(V)3.1 by ProTxII. Toxicon. 2010 Sep 15;56(4):624-36. doi: 10.1016/j.toxicon.2010.06.009. Epub 2010 Jun 23.
Ref 66 Crystallographic insights into sodium-channel modulation by the 4 subunit. Proc Natl Acad Sci U S A. 2013 Dec 17;110(51):E5016-24. doi: 10.1073/pnas.1314557110. Epub 2013 Dec 2.
Ref 67 Block of T-type calcium channels by protoxins I and II. Mol Brain. 2014 May 9;7:36. doi: 10.1186/1756-6606-7-36.
Ref 68 High Proteolytic Resistance of Spider-Derived Inhibitor Cystine Knots. Int J Pept. 2015;2015:537508. doi: 10.1155/2015/537508. Epub 2015 Dec 30.
Ref 69 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 70 Binary architecture of the Nav1.2-2 signaling complex. Elife. 2016 Feb 19;5:e10960. doi: 10.7554/eLife.10960.
Ref 71 Insensitivity to pain induced by a potent selective closed-state Nav1.7 inhibitor. Sci Rep. 2017 Jan 3;7:39662. doi: 10.1038/srep39662.
Ref 72 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 73 Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014 Aug 14;57(15):6623-31. doi: 10.1021/jm500687u. Epub 2014 Jul 24.
Ref 74 Interaction of Tarantula Venom Peptide ProTx-II with Lipid Membranes Is a Prerequisite for Its Inhibition of Human Voltage-gated Sodium Channel NaV1.7. J Biol Chem. 2016 Aug 12;291(33):17049-65. doi: 10.1074/jbc.M116.729095. Epub 2016 Jun 16.
Ref 75 Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell. 2019 Feb 7;176(4):702-715.e14. doi: 10.1016/j.cell.2018.12.018. Epub 2019 Jan 17.
Ref 76 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.
Ref 77 A Tale of Toxin Promiscuity: The Versatile Pharmacological Effects of Hcr 1b-2 Sea Anemone Peptide on Voltage-Gated Ion Channels. Mar Drugs. 2022 Feb 17;20(2):147. doi: 10.3390/md20020147.
Ref 78 APETx4, a Novel Sea Anemone Toxin and a Modulator of the Cancer-Relevant Potassium Channel K(V)10.1. Mar Drugs. 2017 Sep 13;15(9):287. doi: 10.3390/md15090287.
Ref 79 Tarantula toxin ProTx-I differentiates between human T-type voltage-gated Ca2+ Channels Cav3.1 and Cav3.2. J Pharmacol Sci. 2010;112(4):452-8. doi: 10.1254/jphs.09356fp. Epub 2010 Mar 30.
Ref 80 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 81 Mutational analysis of ProTx-I and the novel venom peptide Pe1b provide insight into residues responsible for selective inhibition of the analgesic drug target Na(V)1.7. Biochem Pharmacol. 2020 Nov;181:114080. doi: 10.1016/j.bcp.2020.114080. Epub 2020 Jun 6.
Ref 82 A tarantula-venom peptide antagonizes the TRPA1 nociceptor ion channel by binding to the S1-S4 gating domain. Curr Biol. 2014 Mar 3;24(5):473-83. doi: 10.1016/j.cub.2014.01.013. Epub 2014 Feb 13.
Ref 83 Multitarget nociceptor sensitization by a promiscuous peptide from the venom of the King Baboon spider. Proc Natl Acad Sci U S A. 2022 Feb 1;119(5):e2110932119. doi: 10.1073/pnas.2110932119.
Ref 84 Solution structure and functional characterization of jingzhaotoxin-XI: a novel gating modifier of both potassium and sodium channels. Biochemistry. 2006 Dec 26;45(51):15591-600. doi: 10.1021/bi061457+.
Ref 85 Jingzhaotoxin-35, a novel gating-modifier toxin targeting both Nav1.5 and Kv2.1 channels. Toxicon. 2014 Dec 15;92:90-6. doi: 10.1016/j.toxicon.2014.10.008. Epub 2014 Oct 15.
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.