Cloning of subunits of convulxin, a collagen-like platelet-aggregating protein from Crotalus durissus terrificus venom
Open Access
- 15 July 1998
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 333 (2) , 389-393
- https://doi.org/10.1042/bj3330389
Abstract
Convulxin (CVX) is a potent platelet-aggregating glycoprotein from the venom of the snake Crotalus durissus terrificus. It consists of two subunits, α and β, joined by disulphide bridges in a hexameric structure. A cDNA library from venom gland was constructed in the vector pT3T7. The cloned cDNAs encoding the two chains of CVX were sequenced. Both are preceded by an identical 23-amino acid peptide signal sequence and encode sequences of 135 amino acids for the α chain and 125 amino acids for the β chain. These polypeptides include a carbohydrate-recognition domain (CRD) in which some of the specific amino acids required for binding Ca2+ and galactose or mannose are absent. The presence of such a domain means that CVX can be included in the family of C-type lectins along with other snake venom proteins, although it is not a true lectin. Assuming that the localization of intracatenary disulphide bridges of each CVX chain is similar to that of the CRD and that an intercatenary bridge between the α and β chains is similar to that of the C-type lectin botrocetin, we postulate the existence of an additional intercatenary bridge, which explains the tridimeric structure (αβ)3 of CVX.Keywords
This publication has 23 references indexed in Scilit:
- Adhesion and Activation of Human Platelets Induced by Convulxin Involve Glycoprotein VI and Integrin α2ॆ1Journal of Biological Chemistry, 1997
- A Novel Association of Fc Receptor γ-Chain with Glycoprotein VI and Their Co-expression as a Collagen Receptor in Human PlateletsJournal of Biological Chemistry, 1997
- cDNA Cloning of IX/X-BP, a Heterogeneous Two-Chain Anticoagulant Protein from Snake VenomBiochemical and Biophysical Research Communications, 1996
- Primary Structure of Alboaggregin-B Purified from the Venom ofTrimeresurus albolabrisBiochemical and Biophysical Research Communications, 1996
- Binding of a Novel 50-kilodalton Alboaggregin from Trimeresurus albolabris and Related Viper Venom Proteins to the Platelet Membrane Glycoprotein Ib-IX-V Complex. Effect on Platelet Aggregation and Glycoprotein Ib-Mediated Platelet ActivationBiochemistry, 1996
- Isolation, Characterization and Amino Acid Sequence of Echicetin β Subunit, a Specific Inhibitor of von Willebrand Factor and Thrombin Interaction with Glycoprotein IbBiochemical and Biophysical Research Communications, 1994
- A simple PCR method for screening cDNA libraries.Genome Research, 1994
- III — Isolation and characterization of the α and β subunits of the platelet-activating glycoprotein from the venom of Crotalus durissus cascavellaBiochimie, 1985
- II — Subunit structure of a potent platelet-activating glycoprotein isolated from the venom of Crotalus durissus cascavellaBiochimie, 1984
- I - Isolation and electron microscope studies of a potent platelet-aggregating glycoprotein from the venom of Crotalus durissus cascavellaBiochimie, 1983