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- W2391975143 abstract "The recently discovered coagulation factor Ⅸ/factor Ⅹ binding protein family is widely present in the venom of viperidae snake, which is an unique subfamily in the C type animal lectin superfamily. The proteins of this family are non enzymatic anticoagulants that bind to the Gla domain regions of factor Ⅸ or factor Ⅹ and form 1∶1 complexes with factor Ⅸ or factor Ⅹ in the presence of Ca 2+ ions. They are heterodimeric proteins consisting of two highly homologous peptide chains linked by a single disulfide bridge. Each chain contains one Ca 2+ binding site and an intrachain disulfide bonding pattern similar to those of C type carbohydrate recognition domain. The amino acid sequences of this family exhibit high homology amid them. The crystal structure of habu coagulation factors Ⅸ/Ⅹ binding protein has been determined. It is an intertwined dimer with a central loop projecting into the adjoining chain. Excluding this loop, each chain has a fold similar to rat mannose binding protein." @default.
- W2391975143 created "2016-06-24" @default.
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- W2391975143 date "2000-01-01" @default.
- W2391975143 modified "2023-09-26" @default.
- W2391975143 title "Progress in Research of the Coagulation Factor IX/Factor X-binding Protein Family." @default.
- W2391975143 hasPublicationYear "2000" @default.
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