Factor Xa: Difference between revisions

Line 11:

===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> The Gla domain is responsible for the high-affinity binding of calcium ions and interactions with phospholipid membrane surfaces. Recent crystal structures suggest that the N-terminal epidermal growth factor (EGF)-like domain is flexibly, while the second EGF domain maintains contacts with the catalytic domain.

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 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 3D structures of several Gla domains have been solved.[4][5] Calcium ions induce conformational changes in the Gla domain and are necessary for the Gla domain to fold properly. A common structural feature of functional Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane.[5]

The Gla domain is responsible for the high-affinity binding of calcium ions and interactions with phospholipid membrane surfaces.

Recent crystal structures suggest that the N-terminal epidermal growth factor (EGF)-like domain is flexibly, while the second EGF domain maintains contacts with the catalytic domain.

===Heavy Chain===

Factor Xa: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 11: / Line 11: @@
 ===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> The Gla domain is responsible for the high-affinity binding of calcium ions and interactions with phospholipid membrane surfaces. Recent crystal structures suggest that the N-terminal epidermal growth factor (EGF)-like domain is flexibly, while the second EGF domain maintains contacts with the catalytic domain.
+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 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 3D structures of several Gla domains have been solved.[4][5] Calcium ions induce conformational changes in the Gla domain and are necessary for the Gla domain to fold properly. A common structural feature of functional Gla domains is the clustering of N-terminal hydrophobic residues into a hydrophobic patch that mediates interaction with the cell surface membrane.[5]
+The Gla domain is responsible for the high-affinity binding of calcium ions and interactions with phospholipid membrane surfaces.
+Recent crystal structures suggest that the N-terminal epidermal growth factor (EGF)-like domain is flexibly, while the second EGF domain maintains contacts with the catalytic domain.
 ===Heavy Chain===