Factor IX: Difference between revisions
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The first cleave is at Arg145, generating an inactive FIXα. The second cleavage is at Arg180 results in a catalytically active molecule FIXaβ. This resulting heterodimer is held by a disulfide bridge at Cys132-Cys289. The <scene name='Factor_IX/Ixstructure_chainc/2'>serine protease</scene> contains a catalytic triad of <scene name='Factor_IX/Ixstructure_catalytictriad/2'>His221, Asp269, and Ser365</scene>. Upon cleave at Arg180, Val181 can form a salt bridge with Asp364, which is a characteristic of active <scene name='Factor_IX/Ixstructure_chainc/2'>serine proteases</scene>. The active FIXa, can then interact with its cofactor, FVIIIa, to form a membrane-bound Xase complex, which activated FX to FXa. | The first cleave is at Arg145, generating an inactive FIXα. The second cleavage is at Arg180 results in a catalytically active molecule FIXaβ. This resulting heterodimer is held by a disulfide bridge at Cys132-Cys289. The <scene name='Factor_IX/Ixstructure_chainc/2'>serine protease</scene> contains a catalytic triad of <scene name='Factor_IX/Ixstructure_catalytictriad/2'>His221, Asp269, and Ser365</scene>. Upon cleave at Arg180, Val181 can form a salt bridge with Asp364, which is a characteristic of active <scene name='Factor_IX/Ixstructure_chainc/2'>serine proteases</scene>. The active FIXa, can then interact with its cofactor, FVIIIa, to form a membrane-bound Xase complex, which activated FX to FXa. | ||
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