Factor Xa: Difference between revisions

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===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). <ref name="GLA1">PMID:3106112</ref> <ref name="Gla2">PMID:2183788</ref> This domain begins at the N-terminus of the protein and ends with a conserved aromatic residue. There is also a conserved Gla-X(3)-Gla-X-Cys motif <ref name="GLA seq">PMID: 3317405</ref> is located in the middle of the GLA domain, and appears to be important for recognition by the vitamin K-dependent carboxylase. The Gla residues are responsible for the high-affinity binding of calcium ions. Based on 3D structures of several Gla domains it that the binding of calcium ions induce conformational changes in the domain and are necessary for proper folding of this region. <ref name="GLA Cal">PMID 7713897</ref>A common structural feature of Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane. <ref name="GLA struct">PMID 8663165</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). <ref name="GLA1">PMID:3106112</ref> <ref name="Gla2">PMID:2183788</ref> This domain begins at the N-terminus of the protein and ends with a conserved aromatic residue. There is also a conserved Gla-X(3)-Gla-X-Cys motif <ref name="GLA seq">PMID: 3317405</ref>, located in the middle of the GLA domain, and appears to be important for recognition by the vitamin K-dependent carboxylase. The Gla residues are responsible for the high-affinity binding of calcium ions. Based on 3D structures of several Gla domains it that the binding of calcium ions induce conformational changes in the domain and are necessary for proper folding of this region. <ref name="GLA Cal">PMID 7713897</ref>A common structural feature of Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane. <ref name="GLA struct">PMID 8663165</ref> The Gla domain enables factor X/Xa to bind phospholipid (i.e. cell surfaces) in a calcium dependent manner; a requirement for assembly of the prothrombinase complex.

Factor Xa: Difference between revisions

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Revision as of 22:40, 2 April 2011 view source Jacqueline Gertz (talk \| contribs) 254 edits →Light Chain ← Older edit		Revision as of 23:59, 2 April 2011 view source Jacqueline Gertz (talk \| contribs) 254 edits →Light Chain Newer edit →
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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). <ref name="GLA1">PMID:3106112</ref> <ref name="Gla2">PMID:2183788</ref> This domain begins at the N-terminus of the protein and ends with a conserved aromatic residue. There is also a conserved Gla-X(3)-Gla-X-Cys motif <ref name="GLA seq">PMID: 3317405</ref> is located in the middle of the GLA domain, and appears to be important for recognition by the vitamin K-dependent carboxylase. The Gla residues are responsible for the high-affinity binding of calcium ions. Based on 3D structures of several Gla domains it that the binding of calcium ions induce conformational changes in the domain and are necessary for proper folding of this region. <ref name="GLA Cal">PMID 7713897</ref>A common structural feature of Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane. <ref name="GLA struct">PMID 8663165</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). <ref name="GLA1">PMID:3106112</ref> <ref name="Gla2">PMID:2183788</ref> This domain begins at the N-terminus of the protein and ends with a conserved aromatic residue. There is also a conserved Gla-X(3)-Gla-X-Cys motif <ref name="GLA seq">PMID: 3317405</ref>, located in the middle of the GLA domain, and appears to be important for recognition by the vitamin K-dependent carboxylase. The Gla residues are responsible for the high-affinity binding of calcium ions. Based on 3D structures of several Gla domains it that the binding of calcium ions induce conformational changes in the domain and are necessary for proper folding of this region. <ref name="GLA Cal">PMID 7713897</ref>A common structural feature of Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane. <ref name="GLA struct">PMID 8663165</ref> The Gla domain enables factor X/Xa to bind phospholipid (i.e. cell surfaces) in a calcium dependent manner; a requirement for assembly of the prothrombinase complex.