General Information of This Target
Target ID
BTDT00057
Target Name
Potassium voltage-gated channel subfamily A member 1
Target Bioclass
Transporter and channel
Uniprot ID
P16388
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 ID
16485
Synonym
MBK1; MKI; Voltage-gated potassium channel subunit Kv1.1
Sequence
MTVMSGENADEASTAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPN
TLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFY
ELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILIS
IVIFCLETLPELKDDKDFTGTIHRIDNTTVIYTSNIFTDPFFIVETLCIIWFSFELVVRF
FACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVF
RIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIP
DAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETE
GEEQAQLLHVSSPNLASDSDLSRRSSSTISKSEYMEIEEDMNNSIAHYRQANIRTGNCTT
ADQNCVNKSKLLTDV

    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 and the central nervous system, but also in the kidney. Contributes to the regulation of the membrane potential and nerve signaling, and prevents neuronal hyperexcitability. 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. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of 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. Homotetrameric KCNA1 forms a delayed- rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure. In contrast, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation. Regulates neuronal excitability in hippocampus, especially in mossy fibers and medial perforant path axons, preventing neuronal hyperexcitability. May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons. May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) release. Plays a role in regulating the generation of action potentials and preventing hyperexcitability in myelinated axons of the vagus nerve, and thereby contributes to the regulation of heart contraction. Required for normal neuromuscular responses. Regulates the frequency of neuronal action potential firing in response to mechanical stimuli, and plays a role in the perception of pain caused by mechanical stimuli, but does not play a role in the perception of pain due to heat stimuli. Required for normal responses to auditory stimuli and precise location of sound sources, but not for sound perception. The use of toxins that block specific channels suggest that it contributes to the regulation of the axonal release of the neurotransmitter dopamine. Required for normal postnatal brain development and normal proliferation of neuronal precursor cells in the brain. Plays a role in the reabsorption of Mg(2+) in the distal convoluted tubules in the kidney and in magnesium ion homeostasis, probably via its effect on the membrane potential.

    Click to Show/Hide
Taxonomy ID
10090
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Mammalia
Order: Rodentia
Family: Muridae
Genus: Mus
Species: Mus musculus
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Dissociation constant
>25 nM
[1], [2], [3], [4]
 Toxin Info    Potassium channel toxin ShK ([pTyrMe][AEEA]) Dissociation constant
0.112 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([Apa][AEEA]) Dissociation constant
0.142 nM
[5]
 Toxin Info    Potassium channel toxin ShK (Y[AEEA] Dissociation constant
0.159 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([Pmp2Et]D[AEEA]) Dissociation constant
0.166 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([pTyr2Me][AEEA]) Dissociation constant
0.175 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([Cpa][AEEA]) Dissociation constant
0.319 nM
[5]
 Toxin Info    Potassium channel toxin alpha-KTx 23.1 Dissociation constant
0.8 nM
[6]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA]) Dissociation constant
1 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([Pmp2Et][AEEA]) Dissociation constant
1.1 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([PmpEtD][AEEA]) Dissociation constant
1.1 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([PmpD][AEEA]) Dissociation constant
1.4 nM
[5]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) Dissociation constant
1.8 nM
[5]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) Dissociation constant
7 nM
[5]
 Toxin Info    Potassium channel toxin Bgk (F6A) Dissociation constant
7.3 nM
[7]
 Toxin Info    Kappa-actitoxin-Bgr1a Dissociation constant
17 nM
[7]
 Toxin Info    Potassium channel toxin ShK ([pTyrD][AEEA]) Dissociation constant
39 nM
[5]
 Toxin Info    Potassium channel toxin Bgk (Q24A) Dissociation constant
44 nM
[7]
 Toxin Info    Potassium channel toxin Bgk (W5A) Dissociation constant
61 nM
[7]
 Toxin Info    Potassium channel toxin Bgk (N19A) Dissociation constant
97 nM
[7]
 Toxin Info    Potassium channel toxin Bgk (H13A) Dissociation constant
109 nM
[7]
 Toxin Info    Potassium channel toxin Bgk (Y26A) Dissociation constant
210 nM
[7]
 Toxin Info    Potassium channel toxin Bgk (S23A) Dissociation constant
920 nM
[7]
 Toxin Info    Potassium channel toxin alpha-KTx 10.2 Dissociation constant
1 μM
[11]
 Toxin Info    Potassium channel toxin Bgk (K25A) Dissociation constant
5.497 μM
[7]
 Toxin Info    Toxin II.10.4 (T7P,D9Q) Dissociation constant
7.4 μM
[12]
 Toxin Info    Potassium channel toxin alpha-KTx 10.1 Dissociation constant
24.4 μM
[12]
 Toxin Info    MgTX (K28A) Inhibition rate . [13]
 Toxin Info    Toxin MeKTx13-3 (D19K) Inhibition rate . [14]
 Toxin Info    Toxin MeKTx13-3 (K6D,D19K) Inhibition rate . [14]
 Toxin Info    Pi1 (K24A,Y33[pTyr]) Inhibition rate . [15]
 Toxin Info    Pi1 (K24A,Y33A) Inhibition rate . [15]
 Toxin Info    Anuroctoxin (F32T) Inhibition rate . [16]
 Toxin Info    Anuroctoxin (N17A) Inhibition rate . [16]
 Toxin Info    Anuroctoxin (N17A,F32T) Inhibition rate . [16]
 Toxin Info    Neurotoxin HsTX1 (R14[Abu]) Inhibition rate . [17]
 Toxin Info    ShKT domain-containing protein Inhibition rate . [18], [19]
 Toxin Info    Jingzhaotoxin F7-15.33 Inhibition rate . [20]
 Toxin Info    Potassium channel toxin alpha-KTx 2.1 Inhibition rate . [3]
 Toxin Info    Potassium channel toxin alpha-KTx 23.2 Inhibition rate . [21]
 Toxin Info    Potassium channel toxin alpha-KTx 4.6 Inhibition rate . [22]
 Toxin Info    Potassium channel toxin alpha-KTx 6.12 Inhibition rate . [23]
 Toxin Info    Scorpine-like peptide Ev37 Inhibition rate . [24]
 Toxin Info    Mu-theraphotoxin-Pspp1 Inhibition rate . [25]
 Toxin Info    Potassium channel toxin alpha-KTx 2.13 Inhibition rate . [26]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 Inhibition rate
<50 %
[27], [28]
 Toxin Info    Beta-defensin 1 Inhibition rate
3 %
[29]
 Toxin Info    Beta-defensin 103 Inhibition rate
5 %
[30]
 Toxin Info    Kappa-theraphotoxin-Sc1a Inhibition rate
8 %
[31]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA],Q16K) Inhibition rate
10 %
[32]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA],Q16K,F27[Nle]) Inhibition rate
10 %
[32]
 Toxin Info    Kappa-theraphotoxin-Hm2a Inhibition rate
10 %
[31]
 Toxin Info    Delta-theraphotoxin-Hm1a Inhibition rate
12 %
[31- 35]
 Toxin Info    Fungal defensin plectasin Inhibition rate
16 %
[36]
 Toxin Info    Beta-defensin 3 Inhibition rate
19 %
[37]
 Toxin Info    Beta-defensin 104 Inhibition rate
19 %
[30]
 Toxin Info    Neurotoxin HsTX1 Inhibition rate
20 %
[17]
 Toxin Info    Potassium channel toxin alpha-KTx J123 Inhibition rate
20 %
[38]
 Toxin Info    Potassium channel toxin Sp4 Inhibition rate
20.85 %
[39]
 Toxin Info    Potassium channel toxin Sp4 Inhibition rate
21 %
[39]
 Toxin Info    Defensin BmKDfsin4 Inhibition rate
25 %
[40]
 Toxin Info    Potassium channel toxin KTx1 Inhibition rate
40 %
[41]
 Toxin Info    Potassium channel toxin KTx1 Inhibition rate
40 %
[41]
 Toxin Info    Kunitz-type serine protease inhibitor Hg1 Inhibition rate
45 %
[28]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin K Effective concentration 50
0.03 nM
[42]
 Toxin Info    Kunitz-type serine protease inhibitor homolog delta-dendrotoxin Effective concentration 50
1.8 nM
[42]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin I Effective concentration 50
7.4 nM
[42]
 Toxin Info    Kunitz-type serine protease inhibitor homolog alpha-dendrotoxin Effective concentration 50
9.4 nM
[42]
 Toxin Info    Kappa-stichotoxin-She3a IC50
0.016 nM
[43]
 Toxin Info    ShK (Q16K)-Ala IC50
0.0215 nM
[32]
 Toxin Info    Potassium channel toxin ShK (M21I) IC50
0.14 nM
[32]
 Toxin Info    OsK1 (E15K,K19D) IC50
0.19 nM
[44]
 Toxin Info    Potassium channel toxin ShK ([Pmp][AEEA]) IC50
0.279 nM
[45]
 Toxin Info    OsK1 (E16K,K20D) IC50
0.4 nM
[46]
 Toxin Info    Potassium channel toxin alpha-KTx 3.7 IC50
0.6 nM
[46]
 Toxin Info    OsK1 (E16K) IC50
0.63 nM
[46]
 Toxin Info    Toxin MeKTx13-3 (G11R,I28T,D33H) IC50
0.65 nM
[47]
 Toxin Info    Defensin, beta 104 IC50
0.83 nM
[48]
 Toxin Info    ShK-Lys IC50
0.942 nM
[49]
 Toxin Info    MTX (N21Y,A22G,I25M,K27R,S28K,Y32N,G33R) IC50
1 nM
[50]
 Toxin Info    PBTx3 (N24F) IC50
1.327 nM
[48]
 Toxin Info    Potassium channel toxin ShK (K22[Dap]) IC50
1.8 nM
[43]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA],M21[Nle]) IC50
2.2 nM
[45]
 Toxin Info    OsK1 (K20D) IC50
2.95 nM
[46]
 Toxin Info    Kunitz-type serine protease inhibitor homolog dendrotoxin I IC50
3.1 nM
[51]
 Toxin Info    [P12,K16,D20]- OsK1 IC50
3.18 nM
[46]
 Toxin Info    [pTyr][AEEA]RSCIDTIPKSRCTAFQCKHSMKYRLSFCRKTCGTC ([pTyr][AEEA]) IC50
6.9 nM
[45]
 Toxin Info    Potassium channel toxin ShK ([pTyr][AEEA]) IC50
7 nM
[45]
 Toxin Info    Potassium channel toxin alpha-KTx 6.3 IC50
7 nM
[50]
 Toxin Info    Potassium channel toxin ShK ([Ppa][AEEA],M21[Nle]) IC50
22 nM
[45]
 Toxin Info    OsK1 (E16K,K20D,T36Y) IC50
34.4 nM
[46]
 Toxin Info    ScyTx (F2V,R6K,Q9E,D24V) IC50
160 nM
[52]
 Toxin Info    OsK1 (E16A,K20D) IC50
365 nM
[44]
 Toxin Info    Potassium channel toxin alpha-KTX 12 Sp2 IC50
485 nM
[53]
 Toxin Info    Potassium channel toxin alpha-KTX 12 Sp2 IC50
485 nM
[53]
 Toxin Info    Leiurotoxin I-like toxin P05 (R6K,Q9E,K20V,K25A,E27K) IC50
26.6 μM
[52]
References
Ref 1 Charybdotoxin and noxiustoxin, two homologous peptide inhibitors of the K+ (Ca2+) channel. FEBS Lett. 1988 Jan 4;226(2):280-4. doi: 10.1016/0014-5793(88)81439-x.
Ref 2 Synthetic peptides corresponding to the sequence of noxiustoxin indicate that the active site of this K+ channel blocker is located on its amino-terminal portion. J Neural Transm. 1989;77(1):11-20. doi: 10.1007/BF01255815.
Ref 3 Pharmacological characterization of five cloned voltage-gated K+ channels, types Kv1.1, 1.2, 1.3, 1.5, and 3.1, stably expressed in mammalian cell lines. Mol Pharmacol. 1994 Jun;45(6):1227-34.
Ref 4 Determination of the three-dimensional solution structure of noxiustoxin: analysis of structural differences with related short-chain scorpion toxins. Biochemistry. 1995 Dec 26;34(51):16563-73. doi: 10.1021/bi00051a004.
Ref 5 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 6 Vm24, a natural immunosuppressive peptide, potently and selectively blocks Kv1.3 potassium channels of human T cells. Mol Pharmacol. 2012 Sep;82(3):372-82. doi: 10.1124/mol.112.078006. Epub 2012 May 23.
Ref 7 Structure of the BgK-Kv1.1 complex based on distance restraints identified by double mutant cycles. Molecular basis for convergent evolution of Kv1 channel blockers. J Biol Chem. 2002 Oct 4;277(40):37406-13. doi: 10.1074/jbc.M206205200. Epub 2002 Jul 19.
Ref 8 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 9 Letter: An anti-inflammatory peptide from bee venom. Nature. 1973 Sep 21;245(5421):163-4. doi: 10.1038/245163a0.
Ref 10 Mast cell degranulating peptide: a multi-functional neurotoxin. J Pharm Pharmacol. 1990 Jul;42(7):457-61. doi: 10.1111/j.2042-7158.1990.tb06595.x.
Ref 11 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 12 Cobatoxin 1 from Centruroides noxius scorpion venom: chemical synthesis, three-dimensional structure in solution, pharmacology and docking on K+ channels. Biochem J. 2004 Jan 1;377(Pt 1):37-49. doi: 10.1042/BJ20030977.
Ref 13 Recombinant expression of margatoxin and agitoxin-2 in Pichia pastoris: an efficient method for production of KV1.3 channel blockers. PLoS One. 2012;7(12):e52965. doi: 10.1371/journal.pone.0052965. Epub 2012 Dec 26.
Ref 14 Toxin acidic residue evolutionary function-guided design of de novo peptide drugs for the immunotherapeutic target, the Kv1.3 channel. Sci Rep. 2015 May 8;5:9881. doi: 10.1038/srep09881.
Ref 15 The 'functional' dyad of scorpion toxin Pi1 is not itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels. Biochem J. 2004 Jan 1;377(Pt 1):25-36. doi: 10.1042/BJ20030115.
Ref 16 An engineered scorpion toxin analogue with improved Kv1.3 selectivity displays reduced conformational flexibility. Sci Rep. 2015 Dec 22;5:18397. doi: 10.1038/srep18397.
Ref 17 A potent and Kv1.3-selective analogue of the scorpion toxin HsTX1 as a potential therapeutic for autoimmune diseases. Sci Rep. 2014 Mar 28;4:4509. doi: 10.1038/srep04509.
Ref 18 Kv1.3 channel-blocking immunomodulatory peptides from parasitic worms: implications for autoimmune diseases. FASEB J. 2014 Sep;28(9):3952-64. doi: 10.1096/fj.14-251967. Epub 2014 Jun 2.
Ref 19 The genome and transcriptome of the zoonotic hookworm Ancylostoma ceylanicum identify infection-specific gene families. Nat Genet. 2015 Apr;47(4):416-22. doi: 10.1038/ng.3237. Epub 2015 Mar 2.
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 Vm23 and vm24, two scorpion peptides that block human t-lymphocyte potassium channels (sub-type kv1.3) with high selectivity and decrease the in vivo dth-responses in rats.
Ref 22 Tst26, a novel peptide blocker of Kv1.2 and Kv1.3 channels from the venom of Tityus stigmurus. Toxicon. 2009 Sep 15;54(4):379-89. doi: 10.1016/j.toxicon.2009.05.023. Epub 2009 Jun 3.
Ref 23 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 24 Expression and characterization of a novel scorpine-like peptide Ev37, from the scorpion Euscorpiops validus. Protein Expr Purif. 2013 Mar;88(1):127-33. doi: 10.1016/j.pep.2012.12.004. Epub 2012 Dec 20.
Ref 25 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 26 A selective blocker of Kv1.2 and Kv1.3 potassium channels from the venom of the scorpion Centruroides suffusus suffusus. Biochem Pharmacol. 2008 Oct 30;76(9):1142-54. doi: 10.1016/j.bcp.2008.08.018. Epub 2008 Aug 22.
Ref 27 Transcriptome analysis of the venom gland of the Mexican scorpion Hadrurus gertschi (Arachnida: Scorpiones). BMC Genomics. 2007 May 16;8:119. doi: 10.1186/1471-2164-8-119.
Ref 28 Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family. J Biol Chem. 2012 Apr 20;287(17):13813-21. doi: 10.1074/jbc.M112.343996. Epub 2012 Feb 21.
Ref 29 Human beta-defensin 1, a new animal toxin-like blocker of potassium channel. Toxicon. 2016 Apr;113:1-6. doi: 10.1016/j.toxicon.2016.02.007. Epub 2016 Feb 5.
Ref 30 Pharmacological characterization of human beta-defensins 3 and 4 on potassium channels: Evidence of diversity in beta-defensin-potassium channel interactions. Peptides. 2018 Oct;108:14-18. doi: 10.1016/j.peptides.2018.08.005. Epub 2018 Aug 16.
Ref 31 Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol Pharmacol. 2002 Jul;62(1):48-57. doi: 10.1124/mol.62.1.48.
Ref 32 Development of highly selective Kv1.3-blocking peptides based on the sea anemone peptide ShK. Mar Drugs. 2015 Jan 16;13(1):529-42. doi: 10.3390/md13010529.
Ref 33 Selective spider toxins reveal a role for the Nav1.1 channel in mechanical pain. Nature. 2016 Jun 23;534(7608):494-9. doi: 10.1038/nature17976. Epub 2016 Jun 6.
Ref 34 A selective Na(V)1.1 activator with potential for treatment of Dravet syndrome epilepsy. Biochem Pharmacol. 2020 Nov;181:113991. doi: 10.1016/j.bcp.2020.113991. Epub 2020 Apr 23.
Ref 35 Selective Na(V)1.1 activation rescues Dravet syndrome mice from seizures and premature death. Proc Natl Acad Sci U S A. 2018 Aug 21;115(34):E8077-E8085. doi: 10.1073/pnas.1804764115. Epub 2018 Aug 3.
Ref 36 Plectasin, first animal toxin-like fungal defensin blocking potassium channels through recognizing channel pore region. Toxins (Basel). 2015 Jan 5;7(1):34-42. doi: 10.3390/toxins7010034.
Ref 37 Mouse -Defensin 3, A Defensin Inhibitor of Both Its Endogenous and Exogenous Potassium Channels. Molecules. 2018 Jun 20;23(6):1489. doi: 10.3390/molecules23061489.
Ref 38 Characterization of a new Kv1.3 channel-specific blocker, J123, from the scorpion Buthus martensii Karsch. Peptides. 2008 Sep;29(9):1514-20. doi: 10.1016/j.peptides.2008.04.021. Epub 2008 May 13.
Ref 39 Cloning, expression and identification of KTX-Sp4, a selective Kv1.3 peptidic blocker from Scorpiops pococki. Cell Biosci. 2017 Nov 6;7:60. doi: 10.1186/s13578-017-0187-x. eCollection 2017.
Ref 40 Scorpion Potassium Channel-blocking Defensin Highlights a Functional Link with Neurotoxin. J Biol Chem. 2016 Mar 25;291(13):7097-106. doi: 10.1074/jbc.M115.680611. Epub 2016 Jan 27.
Ref 41 ImKTx1, a new Kv1.3 channel blocker with a unique primary structure. J Biochem Mol Toxicol. 2011 Jul-Aug;25(4):244-51. doi: 10.1002/jbt.20382. Epub 2011 Feb 9.
Ref 42 The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K+ channel, mKv1.1 (MK-1), when stably expressed in Chinese hamster ovary cells. Br J Pharmacol. 1997 Mar;120(6):1029-34. doi: 10.1038/sj.bjp.0701004.
Ref 43 ShK-Dap22, a potent Kv1.3-specific immunosuppressive polypeptide. J Biol Chem. 1998 Dec 4;273(49):32697-707. doi: 10.1074/jbc.273.49.32697.
Ref 44 Pharmacological profiling of Orthochirus scrobiculosus toxin 1 analogs with a trimmed N-terminal domain. Mol Pharmacol. 2006 Jan;69(1):354-62. doi: 10.1124/mol.105.017210. Epub 2005 Oct 18.
Ref 45 Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes. Mol Pharmacol. 2009 Apr;75(4):762-73. doi: 10.1124/mol.108.052704. Epub 2009 Jan 2.
Ref 46 K+ channel types targeted by synthetic OSK1, a toxin from Orthochirus scrobiculosus scorpion venom. Biochem J. 2005 Jan 1;385(Pt 1):95-104. doi: 10.1042/BJ20041379.
Ref 47 Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease. J Biol Chem. 2008 Jul 4;283(27):19058-65. doi: 10.1074/jbc.M802054200. Epub 2008 May 14.
Ref 48 N-Terminally extended analogues of the K? channel toxin from Stichodactyla helianthus as potent and selective blockers of the voltage-gated potassium channel Kv1.3. FEBS J. 2015 Jun;282(12):2247-59. doi: 10.1111/febs.13294. Epub 2015 Apr 23.
Ref 49 A C-terminally amidated analogue of ShK is a potent and selective blocker of the voltage-gated potassium channel Kv1.3. FEBS Lett. 2012 Nov 16;586(22):3996-4001. doi: 10.1016/j.febslet.2012.09.038. Epub 2012 Oct 9.
Ref 50 Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins. J Biol Chem. 2004 Dec 31;279(53):55690-6. doi: 10.1074/jbc.M410055200. Epub 2004 Oct 21.
Ref 51 Properties of voltage-gated K+ currents expressed in Xenopus oocytes by mKv1.1, mKv1.2 and their heteromultimers as revealed by mutagenesis of the dendrotoxin-binding site in mKv1.1. Pflugers Arch. 1994 Oct;428(3-4):382-90. doi: 10.1007/BF00724522.
Ref 52 Protein-protein recognition control by modulating electrostatic interactions. J Proteome Res. 2010 Jun 4;9(6):3118-25. doi: 10.1021/pr100027k.
Ref 53 Immunosuppressive effects of a novel potassium channel toxin Ktx-Sp2 from Scorpiops Pocoki. Cell Biosci. 2019 Dec 16;9:99. doi: 10.1186/s13578-019-0364-1. eCollection 2019.
Ref 54 The impact of the fourth disulfide bridge in scorpion toxins of the alpha-KTx6 subfamily. Proteins. 2005 Dec 1;61(4):1010-23. doi: 10.1002/prot.20681.
Ref 55 Design and characterization of a highly selective peptide inhibitor of the small conductance calcium-activated K+ channel, SkCa2. J Biol Chem. 2001 Nov 16;276(46):43145-51. doi: 10.1074/jbc.M106981200. Epub 2001 Aug 29.
Ref 56 Engineering a peptide inhibitor towards the KCNQ1/KCNE1 potassium channel (IKs). Peptides. 2015 Sep;71:77-83. doi: 10.1016/j.peptides.2015.07.002. Epub 2015 Jul 15.
Ref 57 Mechanisms Underlying the Inhibition of KV1.3 Channel by Scorpion Toxin ImKTX58. Mol Pharmacol. 2022 Sep;102(3):150-160. doi: 10.1124/molpharm.121.000480. Epub 2022 Jun 28.
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.