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

研究成果: Article

19 引文 (Scopus)

摘要

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.

原文English
頁(從 - 到)119-126
頁數8
期刊Thrombosis and Haemostasis
83
發行號1
出版狀態Published - 2000 一月 25

指紋

Platelet Glycoprotein GPIb-IX Complex
Venoms
Carrier Proteins
Complementary DNA
Crotalid Venoms
Trimeresurus
C-Type Lectins
Factor X
Snake Venoms
Factor IX
Protein C
Lectins
Disulfides
Organism Cloning
Amino Acid Sequence
Proteins
Nucleotides
Amino Acids
agkicetin

All Science Journal Classification (ASJC) codes

  • Hematology

引用此文

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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.",
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T1 - Glycoprotein Ib-binding protein from the venom of Deinagkistrodon acutus - cDNA sequence, functional characterization, and three-dimensional modeling

AU - Chen, Yuh-Ling

AU - Tsai, Kuo Wei

AU - Chang, Tschining

AU - Hong, Tse-Ming

AU - Tsai, Inn Ho

PY - 2000/1/25

Y1 - 2000/1/25

N2 - 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.

AB - 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.

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