Factor IX: Difference between revisions

The catalytic domain of FIX is composed of two β-<scene name='Factor_IX/Rfnscene/3'>barrel</scene> subdomains that form an active site at their interface. The active site is located at the junction of these β-barrels. The EGF-2 domain is connected to the catalytic domain through a disulfide bridge and is opposite to the active site. There are three disulfide bonds, and the C-terminus contains helical structures that run across the N-terminus of the β-barrel. The catalytic domain contains a calcium binding site that exposes the <scene name='Factor_IX/Rfnscene_5/1'>148-loop</scene> for proteolytic cleavage. This calcium ion is stabilized by Glu-70, Glu-77, Glu-80 and a main chain oxygens of Asn-72 and Glu-75. This site seems to be preformed, unlike the calcium binding sites that are generated in the Gla domain upon calcium binding.  

== References ==

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