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Thromb Haemost 2000; 83(01): 119-126
DOI: 10.1055/s-0037-1613767
Commentary
Schattauer GmbH

Glycoprotein Ib-binding Protein from the Venom of Deinagkistrodon acutus – cDNA Sequence, Functional Characterization, and Three-Dimensional Modeling

Yuh-Ling Chen
1   From the Institute of Biological Chemistry
,
Kuo-Wei Tsai
1   From the Institute of Biological Chemistry
,
Tschining Chang
1   From the Institute of Biological Chemistry
,
Tse-Ming Hong
2   Institute of Biomedical Sciences, Academia Sinica
,
Inn-Ho Tsai
1   From the Institute of Biological Chemistry
3   Institute of Biochemical Sciences, National Taiwan University, Taipei, Taiwan, Republic of China
› Author Affiliations
Further Information

Publication History

Received 12 July 1999

Accepted after revision 23 September 1999

Publication Date:
06 December 2017 (online)

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Summary

Agkicetin-C, a potent glycoprotein Ib antagonist from the venom of the Chinese pit viper, Deinagkistrodon acutus, has been purified and characterized (5). It is a disulfide-linked heterodimer containing subunits of 132 and of 123 amino acid residues. Herein, the complete amino acid sequences were resolved by cloning and nucleotide sequencing of the cDNAs. The sequences of its subunits are homologous to those of other snake venom proteins of the C-type (Ca2+-dependent) lectin superfamily. A three-dimensional model of agkicetin-C was constructed based on the crystal structure of habu coagulation factor IX/X-binding protein. By careful alignment of all the related sequences available and comparing the 3D-model of agkicetin-C with structures of other homologous proteins of different functions, some variable residues of agkicetin-C were identified, which possibly are responsible for the specificity of this distinct subtype of the C-type lectin-like venom proteins.

Keywords

Glycoprotein Ib - snake - modeling - C-lectin
 

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