Factor Xa: Difference between revisions

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===Light Chain===
===Light Chain===
The factor Xa light chain contains a γ-carboxyglutamic acid (Gla) domain [http://en.wikipedia.org/wiki/Gla_domain γ-carboxyglutamic acid (Gla)](11 gla residues) as well as two epidermial growth factor (EGF)-like domains [http://en.wikipedia.org/wiki/Epidermal_growth_factor epidermal growth factor (EGF)].<ref name="EGF">PMID:8355279</ref> Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain is a protein domain that contains post-translational modifications of many glutamate residues by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla). The Gla residues are responsible for the high-affinity binding of calcium ions. <ref name="GLA1">PMID: 3106112, PMID: 2183788</ref>
The factor Xa light chain contains a γ-carboxyglutamic acid (Gla) domain [http://en.wikipedia.org/wiki/Gla_domain γ-carboxyglutamic acid (Gla)](11 gla residues) as well as two epidermial growth factor (EGF)-like domains [http://en.wikipedia.org/wiki/Epidermal_growth_factor epidermal growth factor (EGF)].<ref name="EGF">PMID:8355279</ref> Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain is a protein domain that contains post-translational modifications of many glutamate residues by vitamin K-dependent carboxylation to form gamma-carboxyglutamate (Gla). The Gla residues are responsible for the high-affinity binding of calcium ions. <ref name="GLA1">PMID:3106112</ref>  <ref name="EGF">PMID:2183788</ref>


The GLA domain is responsible for the high-affinity binding of calcium ions. It starts at the N-terminal extremity of the mature form of proteins and ends with a conserved aromatic residue; a conserved Gla-x(3)-Gla-x-Cys motif[3] is found in the middle of the domain which seems to be important for substrate recognition by the carboxylase.
The GLA domain is responsible for the high-affinity binding of calcium ions. It starts at the N-terminal extremity of the mature form of proteins and ends with a conserved aromatic residue; a conserved Gla-x(3)-Gla-x-Cys motif[3] is found in the middle of the domain which seems to be important for substrate recognition by the carboxylase.