General Information of This Target
Target ID
BTDT10038
Target Name
Coagulation factor X
Target Bioclass
Coagulation factor
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N.A.
Toxin Information Related to This Target
                           Toxin Name Activity Data Type Activity Data Reference
 Toxin Info    Lufaxin Dissociation constant
3.86 nM
[1], [2], [3]
 Toxin Info    Phospholipase A2 crotoxin basic subunit CBc IC50
0.7 nM
[4- 16]
 Toxin Info    Basic phospholipase A2 homolog 2 IC50
3 nM
[11- 32]
 Toxin Info    Phospholipase A2 crotoxin basic chain CBa2 IC50
41 nM
[5- 33]
 Toxin Info    Basic phospholipase A2 B IC50
90 nM
[11- 37]
 Toxin Info    Basic phospholipase A2 VRV-PL-VIIIa IC50
130 nM
[11- 50]
 Toxin Info    Kunitz-type serine protease inhibitor taicotoxin IC50
871 nM
[51- 56]
References
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Ref 2 Lufaxin, a novel factor Xa inhibitor from the salivary gland of the sand fly Lutzomyia longipalpis blocks protease-activated receptor 2 activation and inhibits inflammation and thrombosis in vivo. Arterioscler Thromb Vasc Biol. 2012 Sep;32(9):2185-98. doi: 10.1161/ATVBAHA.112.253906. Epub 2012 Jul 12.
Ref 3 The Sand Fly Salivary Protein Lufaxin Inhibits the Early Steps of the Alternative Pathway of Complement by Direct Binding to the Proconvertase C3b-B. Front Immunol. 2017 Aug 31;8:1065. doi: 10.3389/fimmu.2017.01065. eCollection 2017.
Ref 4 Cloning and sequencing of cDNAs encoding the two subunits of Crotoxin. Nucleic Acids Res. 1988 Sep 26;16(18):9050. doi: 10.1093/nar/16.18.9050.
Ref 5 The origin of the diversity of crotoxin isoforms in the venom of Crotalus durissus terrificus. Eur J Biochem. 1994 Jul 1;223(1):161-4. doi: 10.1111/j.1432-1033.1994.tb18978.x.
Ref 6 Molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms. Biochem J. 2004 Jul 1;381(Pt 1):25-34. doi: 10.1042/BJ20040125.
Ref 7 Comparison of crotoxin isoforms reveals that stability of the complex plays a major role in its pharmacological action. Eur J Biochem. 1993 Jun 1;214(2):491-6. doi: 10.1111/j.1432-1033.1993.tb17946.x.
Ref 8 Regulation of epidermal growth factor receptor activity by crotoxin, a snake venom phospholipase A2 toxin. A novel growth inhibitory mechanism. Biochem Pharmacol. 1996 Jun 14;51(11):1535-43. doi: 10.1016/0006-2952(96)00097-4.
Ref 9 Interaction of the neurotoxic and nontoxic secretory phospholipases A2 with the crotoxin inhibitor from Crotalus serum. Eur J Biochem. 2000 Aug;267(15):4799-808. doi: 10.1046/j.1432-1327.2000.01532.x.
Ref 10 Phase I and pharmacokinetics study of crotoxin (cytotoxic PLA(2), NSC-624244) in patients with advanced cancer. Clin Cancer Res. 2002 Apr;8(4):1033-41.
Ref 11 Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct Biol. 2007 Dec 6;7:82. doi: 10.1186/1472-6807-7-82.
Ref 12 Crotoxin: novel activities for a classic beta-neurotoxin. Toxicon. 2010 Jun 1;55(6):1045-60. doi: 10.1016/j.toxicon.2010.01.011. Epub 2010 Jan 28.
Ref 13 Crystal structure of crotoxin reveals key residues involved in the stability and toxicity of this potent heterodimeric -neurotoxin. J Mol Biol. 2011 Sep 16;412(2):176-91. doi: 10.1016/j.jmb.2011.07.027. Epub 2011 Jul 23.
Ref 14 Rattlesnake Phospholipase A2 Increases CFTR-Chloride Channel Current and Corrects ?F508CFTR Dysfunction: Impact in Cystic Fibrosis. J Mol Biol. 2016 Jul 17;428(14):2898-915. doi: 10.1016/j.jmb.2016.05.016. Epub 2016 May 27.
Ref 15 Crotoxin promotes macrophage reprogramming towards an antiangiogenic phenotype. Sci Rep. 2019 Mar 12;9(1):4281. doi: 10.1038/s41598-019-40903-0.
Ref 16 Insights into the role of oligomeric state on the biological activities of crotoxin: crystal structure of a tetrameric phospholipase A2 formed by two isoforms of crotoxin B from Crotalus durissus terrificus venom. Proteins. 2008 Aug 15;72(3):883-91. doi: 10.1002/prot.21980.
Ref 17 Cloning and cDNA sequence analysis of Lys(49) and Asp(49) basic phospholipase A(2) myotoxin isoforms from Bothrops asper. Int J Biochem Cell Biol. 2001 Feb;33(2):127-32. doi: 10.1016/s1357-2725(00)00073-x.
Ref 18 Myotoxin II from Bothrops asper (Terciopelo) venom is a lysine-49 phospholipase A2. Arch Biochem Biophys. 1991 Feb 1;284(2):352-9. doi: 10.1016/0003-9861(91)90307-5.
Ref 19 Solving the microheterogeneity of Bothrops asper myotoxin-II by high-resolution mass spectrometry: Insights into C-terminal region variability in Lys49-phospholipase A(2) homologs. Toxicon. 2022 Apr 30;210:123-131. doi: 10.1016/j.toxicon.2022.02.024. Epub 2022 Mar 3.
Ref 20 A new muscle damaging toxin, myotoxin II, from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1989;27(7):725-33. doi: 10.1016/0041-0101(89)90039-1.
Ref 21 Neutralizing interaction between heparins and myotoxin II, a lysine 49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin region by the use of synthetic peptides and molecular modeling. J Biol Chem. 1994 Nov 25;269(47):29867-73.
Ref 22 Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom. Toxicon. 1994 Nov;32(11):1359-69. doi: 10.1016/0041-0101(94)90408-1.
Ref 23 Autocatalytic acylation of phospholipase-like myotoxins. Biochemistry. 1995 Apr 11;34(14):4670-5. doi: 10.1021/bi00014a021.
Ref 24 Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom--synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region. Eur J Biochem. 1998 Apr 15;253(2):452-61. doi: 10.1046/j.1432-1327.1998.2530452.x.
Ref 25 Pharmacological modulation of edema induced by Lys-49 and Asp-49 myotoxic phospholipases A2 isolated from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1998 Dec;36(12):1861-9. doi: 10.1016/s0041-0101(98)00107-x.
Ref 26 Comparative study of the cytolytic activity of myotoxic phospholipases A2 on mouse endothelial (tEnd) and skeletal muscle (C2C12) cells in vitro. Toxicon. 1999 Jan;37(1):145-58. doi: 10.1016/s0041-0101(98)00171-8.
Ref 27 Bothrops snake myotoxins induce a large efflux of ATP and potassium with spreading of cell damage and pain. Proc Natl Acad Sci U S A. 2010 Aug 10;107(32):14140-5. doi: 10.1073/pnas.1009128107. Epub 2010 Jul 26.
Ref 28 Membrane cholesterol modulates the cytolytic mechanism of myotoxin II, a Lys49 phospholipase A2 homologue from the venom of Bothrops asper. Cell Biochem Funct. 2011 Jul;29(5):365-70. doi: 10.1002/cbf.1758. Epub 2011 Apr 19.
Ref 29 N-terminal domain of Bothrops asper Myotoxin II Enhances the Activity of Endothelin Converting Enzyme-1 and Neprilysin. Sci Rep. 2016 Mar 2;6:22413. doi: 10.1038/srep22413.
Ref 30 Corrigendum: N-terminal domain of Bothrops asper Myotoxin II Enhances the Activity of Endothelin Converting Enzyme-1 and Neprilysin. Sci Rep. 2016 Apr 22;6:24333. doi: 10.1038/srep24333.
Ref 31 Structure of a calcium-independent phospholipase-like myotoxic protein from Bothrops asper venom. Acta Crystallogr D Biol Crystallogr. 1995 May 1;51(Pt 3):311-7. doi: 10.1107/S0907444994011455.
Ref 32 Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin. J Mol Biol. 2005 Jul 15;350(3):416-26. doi: 10.1016/j.jmb.2005.04.072.
Ref 33 Analysis of cDNAs encoding the two subunits of crotoxin, a phospholipase A2 neurotoxin from rattlesnake venom: the acidic non enzymatic subunit derives from a phospholipase A2-like precursor. Biochim Biophys Acta. 1991 Mar 26;1088(3):401-8. doi: 10.1016/0167-4781(91)90132-6.
Ref 34 Cloning of the BPLA(2) Gene from Agkistrodon halys Pallas. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 1996;28(6):579-582.
Ref 35 Diversity of cDNAs encoding phospholipase A2 from Agkistrodon halys pallas venom, and its expression in E. coli. Toxicon. 1998 Aug;36(8):1155-63. doi: 10.1016/s0041-0101(98)00013-0.
Ref 36 Structure of a basic phospholipase A2 from Agkistrodon halys Pallas at 2.13 A resolution. Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):510-21. doi: 10.1107/s0907444997013644.
Ref 37 Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities. Toxicon. 2000 Jul;38(7):901-16. doi: 10.1016/s0041-0101(99)00193-2.
Ref 38 Primary sequence determination of the most basic myonecrotic phospholipase A2 from the venom of Vipera russelli. Toxicon. 1994 Jun;32(6):665-73. doi: 10.1016/0041-0101(94)90336-0.
Ref 39 Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies. Toxicon. 1996 Jan;34(1):99-109. doi: 10.1016/0041-0101(95)00114-x.
Ref 40 Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka. Biomed Res. 2010 Feb;31(1):71-81. doi: 10.2220/biomedres.31.71.
Ref 41 Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelli) venom. Toxicon. 1989;27(2):229-37. doi: 10.1016/0041-0101(89)90136-0.
Ref 42 Antibodies to a phospholipase A2 from Vipera russelli selectively neutralize venom neurotoxicity. Immunology. 1990 Jun;70(2):175-80.
Ref 43 Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from Daboia russelli pulchella at 2.4 A resolution. J Mol Biol. 2000 Mar 3;296(4):1117-26. doi: 10.1006/jmbi.2000.3537.
Ref 44 Regulation of catalytic function by molecular association: structure of phospholipase A2 from Daboia russelli pulchella (DPLA2) at 1.9 A resolution. Acta Crystallogr D Biol Crystallogr. 2001 Dec;57(Pt 12):1793-8. doi: 10.1107/s0907444901014524. Epub 2001 Nov 21.
Ref 45 Design of specific peptide inhibitors of phospholipase A2: structure of a complex formed between Russell's viper phospholipase A2 and a designed peptide Leu-Ala-Ile-Tyr-Ser (LAIYS). Acta Crystallogr D Biol Crystallogr. 2002 Oct;58(Pt 10 Pt 2):1813-9. doi: 10.1107/s0907444902013720. Epub 2002 Sep 28.
Ref 46 Structural basis of phospholipase A2 inhibition for the synthesis of prostaglandins by the plant alkaloid aristolochic acid from a 1.7 A crystal structure. Biochemistry. 2002 Sep 10;41(36):10914-9. doi: 10.1021/bi0258593.
Ref 47 Crystal structure of a complex formed between a snake venom phospholipase A(2) and a potent peptide inhibitor Phe-Leu-Ser-Tyr-Lys at 1.8 A resolution. J Biol Chem. 2002 Oct 25;277(43):41079-85. doi: 10.1074/jbc.M206130200. Epub 2002 Aug 16.
Ref 48 Phospholipase A2 as a target protein for nonsteroidal anti-inflammatory drugs (NSAIDS): crystal structure of the complex formed between phospholipase A2 and oxyphenbutazone at 1.6 A resolution. Biochemistry. 2004 Nov 23;43(46):14577-83. doi: 10.1021/bi0483561.
Ref 49 Crystal structures of the complexes of a group IIA phospholipase A2 with two natural anti-inflammatory agents, anisic acid, and atropine reveal a similar mode of binding. Proteins. 2006 Jul 1;64(1):89-100. doi: 10.1002/prot.20970.
Ref 50 Structures and binding studies of the complexes of phospholipase A2 with five inhibitors. Biochim Biophys Acta. 2015 Apr;1854(4):269-77. doi: 10.1016/j.bbapap.2014.12.017. Epub 2014 Dec 23.
Ref 51 Common evolution of waprin and kunitz-like toxin families in Australian venomous snakes. Cell Mol Life Sci. 2008 Dec;65(24):4039-54. doi: 10.1007/s00018-008-8573-5.
Ref 52 Isolation and physiological characterization of taicatoxin, a complex toxin with specific effects on calcium channels. Toxicon. 1992 Nov;30(11):1343-64. doi: 10.1016/0041-0101(92)90511-3.
Ref 53 Identification and characterisation of Kunitz-type plasma kallikrein inhibitors unique to Oxyuranus sp. snake venoms. Biochimie. 2012 Feb;94(2):365-73. doi: 10.1016/j.biochi.2011.08.003. Epub 2011 Aug 11.
Ref 54 Effect of TaiCatoxin (TCX) on the electrophysiological, mechanical and biochemical characteristics of spontaneously beating ventricular cardiomyocytes. Mol Cell Biochem. 1996 Jul-Aug;160-161:61-6. doi: 10.1007/BF00240032.
Ref 55 A novel small conductance Ca2+-activated K+ channel blocker from Oxyuranus scutellatus taipan venom. Re-evaluation of taicatoxin as a selective Ca2+ channel probe. J Biol Chem. 1997 Aug 8;272(32):19925-30. doi: 10.1074/jbc.272.32.19925.
Ref 56 Taicatoxin inhibits the calcium-dependent slow motility of mammalian outer hair cells. Hear Res. 2005 May;203(1-2):172-9. doi: 10.1016/j.heares.2004.12.003.
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