Glycoprotein Ib-binding protein from the venom of Deinagkistrodon acutus - cDNA sequence, functional characterization, and three-dimensional modeling

Yuh Ling Chen, Kuo Wei Tsai, Tschining Chang, Tse Ming Hong, Inn Ho Tsai

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20 Citations (Scopus)

Abstract

Agkicetin-C, a potent glycoprotein Ib antagonist from the venom of the Chinese pit viper, Deinagkistrodon acutus, has been purified and characterized. 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 super-family. 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.

Original languageEnglish
Pages (from-to)119-126
Number of pages8
JournalThrombosis and Haemostasis
Volume83
Issue number1
Publication statusPublished - 2000 Jan 25

All Science Journal Classification (ASJC) codes

  • Hematology

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