Calcium-binding analysis and molecular modeling reveal echis coagulation factor IX/factor X-binding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins.

Hideko Atoda; Hiroki Kaneko; Hiroshi Mizuno; Takashi Morita

doi:10.1016/s0014-5793(02)03507-x

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Calcium-binding analysis and molecular modeling reveal echis coagulation factor IX/factor X-binding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins.

Hideko Atoda·Hiroki Kaneko·Hiroshi Mizuno·Takashi Morita

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Abstract

Many biologically active heterodimeric proteins of snake venom consist of two C-type lectin-like subunits. One of these proteins, habu IX/X-bp, is a Gla domain-binding protein whose subunits both bind to a Ca2+ ion, with a total of two Ca2+-binding sites. The molecular modeling and Ca2+-binding analysis of echis IX/X-bp revealed that it lacks one of two Ca2+-binding sites, though the folding of this subunit is conserved. It is concluded that heterodimeric C-type lectin-like proteins function independent of Ca2+ and have essentially a similar folding to habu IX/X-bp.

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Amino Acid Sequence Binding Sites Calcium Lectins, C-Type Models, Molecular Molecular Sequence Data Protein Binding Protein Folding Protein Structure, Tertiary Protein Subunits Sequence Homology, Amino Acid Viper Venoms Comparative Study Journal Article Research Support, Non-U.S. Gov't

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Hideko Atoda, Hiroki Kaneko, Hiroshi Mizuno, Takashi Morita. 2002-11-06. Calcium-binding analysis and molecular modeling reveal echis coagulation factor IX/factor X-binding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins.. https://doi.org/10.1016/s0014-5793(02)03507-x

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