Factor VIIa: Difference between revisions
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The Gla domain binds four Ca++ ions and three Mg++ ions arranged in a linear fashion. Ca++ induced changes in the Gla domain are responsible for major structural rearrangements in that region that facilitate binding of FVIIa to membrane<ref>PMID:8844844</ref>. Binding of Ca++ induces an increase in the α-helical content of that region. The EGF1 domain contains one Ca++ binding site believed to be important for TF binding. The protease domain binds bidns one Ca++, one Na+ and two Zn++ ions. The Zn++ ions have been shown to inhibit the activity of FVIIa specifically by reducing its affinity for TF. Ca++ binding in the protease domain, mediated by Glu210 and Glu220, produces subtle local changes presumably important for TF binding. The Na+ binding site is located in a hydrophobic cavity responsible for TF binding<ref>PMID: 16757484 </ref>. | The Gla domain binds four Ca++ ions and three Mg++ ions arranged in a linear fashion. Ca++ induced changes in the Gla domain are responsible for major structural rearrangements in that region that facilitate binding of FVIIa to membrane<ref>PMID:8844844</ref>. Binding of Ca++ induces an increase in the α-helical content of that region. The EGF1 domain contains one Ca++ binding site believed to be important for TF binding. The protease domain binds bidns one Ca++, one Na+ and two Zn++ ions. The Zn++ ions have been shown to inhibit the activity of FVIIa specifically by reducing its affinity for TF. Ca++ binding in the protease domain, mediated by Glu210 and Glu220, produces subtle local changes presumably important for TF binding. The Na+ binding site is located in a hydrophobic cavity responsible for TF binding<ref>PMID: 16757484 </ref>. | ||
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