Factor IX: Difference between revisions

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The Gla domain is situated at the N-terminus of coagulation factor IX, and is evolutionary conserved in other vitamin K dependent proteins such as factor VII, X, and prothrombin. A <scene name='Factor_IX/Gladomain_glamgca/2'>Gla domain</scene> is made up of 10-13 of γ-carboxyglutamic acid residues and requires both <scene name='Factor_IX/Gladomain_1/5'>Ca2+ and Mg2+ </scene> ions for membrane association and stabilization of its active three dimensional conformation (2-4).  
The Gla domain is situated at the N-terminus of coagulation factor IX, and is evolutionary conserved in other vitamin K dependent proteins such as factor VII, X, and prothrombin. A <scene name='Factor_IX/Gladomain_glamgca/2'>Gla domain</scene> is made up of 10-13 of γ-carboxyglutamic acid residues and requires both <scene name='Factor_IX/Gladomain_1/6'>Ca2+ and Mg2+ </scene> ions for membrane association and stabilization of its active three dimensional conformation (2-4).  


In the presence of [[calcium ions the Gla domain]] (Calcium ions 5 and 6 and Gla residues 17 and 21) interacts with serine head group of phosphatidylserine located on the phospholipid membrane (2).  In the absence of metal ions the Gla domain is highly disordered and unstructured which indicated that the metal ions, stabilize the structure (4-6). Three Mg2+ ions, (Mg-1, Mg-7, and Mg-8) are located on the surface of FIX and correspond to FX,  three Ca2+ ions (Ca-1, Ca-7, and Ca-8). Each Mg2+ ion has a bipyramidal coordination with a water molecule (Mg–O in FIX is 2.12 Å, whereas the Ca–O distances in FX is 2.41 Å) and a pair of Gla residues.  
In the presence of [[calcium ions the Gla domain]] (Calcium ions 5 and 6 and Gla residues 17 and 21) interacts with serine head group of phosphatidylserine located on the phospholipid membrane (2).  In the absence of metal ions the Gla domain is highly disordered and unstructured which indicated that the metal ions, stabilize the structure (4-6). Three Mg2+ ions, (Mg-1, Mg-7, and Mg-8) are located on the surface of FIX and correspond to FX,  three Ca2+ ions (Ca-1, Ca-7, and Ca-8). Each Mg2+ ion has a bipyramidal coordination with a water molecule (Mg–O in FIX is 2.12 Å, whereas the Ca–O distances in FX is 2.41 Å) and a pair of Gla residues.  

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Nadia Dorochko, Alexander Berchansky, David Canner, Michal Harel