Blood Coagulation Factor IX/Factor X-Binding Protein

  • Takashi MoritaEmail author


C-type lectin-like proteins of snake have a variety of biological properties, acting for example as an anticoagulant, procoagulant, and agonist/antagonist of platelet activation. Dimerization or oligomer formation of carbohydrate recognition domain (CRD) in C-type lectin by 3D domain swapping generates novel proteins with new functions such as coagulant-, anticoagulant-, and platelet-modulating activities. The structural and functional studies of the first identified C-type lectin-like proteins, IX/X-bp, have been instrumental in defining how new functionally heterodimeric C-type lectin-like proteins are generated from monomeric CRD (carbohydrate recognition domain) in C-type lectin by 3D domain swapping. The crystal structure of IX/X-bp revealed that the two subunits associated by 3 D-domain swapping, and this dimerization resulted in the creation of a concave surface serving as a binding site of Gla domain, the functionally important domain of blood coagulation factors. The strong activities by snaclecs such as IX/X-bp and X-bp are caused by the binding at the Gla domain of factors IX and X. C-type lectin-like proteins of snake venom such as IX/X-bp and its structurally-related proteins recognize various ligands by the higher frequency of mutation in the open reading frames than in the non-coding regions after duplication of a gene.


Snake Venom Carbohydrate Recognition Domain Blood Coagulation Cascade Mannose Binding Protein Hinge Loop 
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© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Department of BiochemistryMeiji Pharmaceutical UniversityTokyoJapan
  2. 2.Department of Host Defense and Biological ResearchJuntendo University School of MedicineTokyoJapan

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