General Information of This Peptide
Peptide ID
BTDP006258
Peptide Name
Phospholipase A2 crotoxin basic subunit CBc
Symonym
Phosphatidylcholine 2-acylhydrolase
Species
Crotalus durissus terrificus (South American rattlesnake)
Uniprot Name
PA2BC_CRODU
Alphafold ID
P62022
3D Structure
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2D Sequence
3D Structure
Source
RSCB PDB: 2QOG
Sequence
MRALWIVAVLLVGVEGHLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCC
FVHDCCYGKLAKCNTKWDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYK
YGYMFYPDSRCRGPSETC
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Sequence Length
138
Mass (Da)
15907
Signal Sequence
MRALWIVAVLLVGVEG
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Sequence Removed Signal Peptide
HLLQFNKMIKFETRKNAIPFYAFYGCYCGWGGRGRPKDATDRCCFVHDCCYGKLAKCNTK
WDIYPYSLKSGYITCGKGTWCEEQICECDRVAAECLRRSLSTYKYGYMFYPDSRCRGPSE
TC
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Disulfide Bond
42-131;44-60;59-111;65-138;66-104;73-97;91-102
PDB ID
2QOG
        Click to Show/Hide the Complete Species Lineage
Kingdom: Metazoa
Phylum: Chordata
Class: Lepidosauria
Order: Squamata
Family: Viperidae
Genus: Crotalus
Species: Crotalus durissus
Full List of Activity Data of This Peptide Toxin
                        Target Name Activity Data Type Activity Data Concentration Note Reference
 Target Info    factor Xa (F10) IC50
0.7 nM
. . [1- 13]
References
Ref 1 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 2 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 3 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 4 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 5 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 6 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 7 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 8 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 9 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 10 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 11 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 12 Crotoxin promotes macrophage reprogramming towards an antiangiogenic phenotype. Sci Rep. 2019 Mar 12;9(1):4281. doi: 10.1038/s41598-019-40903-0.
Ref 13 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.
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