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Kori Jackson Paper 4 Flow Chart 4/7/2014
What Asked: What molecular interactions are integral for the binding of Factor VII to Tissue Factor?
How Asked: What molecular (protein-protein) interactions take place in solution and are integral to in
solution behavior of Factor VII and it’s binding to VIIa and TF. Which domains are important, and how
does Ca2+
affect binding affinity of this system.
Figure 1: Analysis of binding tissue factor complesxes with non-inhibitory anti-tissue factor This was to
see the TF-VII interaction in solution. Binding of TF complexes to anti-tissue factor not affected by
presence of VII. Authors claim that binding of TF complexes to anti-tissue factor reflects concentration of
complexes formed in solution.
Figure 2: Analysis of factor VII binding to Tissue Factor and extracelluar Tissue Factor domain (TF:1-219)
 binding of VII to TF:1-219 had a 10-fold higher Kd than regular TF.
Figure 3: Analysis of des-(1-38)-VII binding to TF and TF:1-219. binding was tighter for TF:1-219 than
regular TF.
Figure 4: Analysis of tissue factor extracellular domain with and without calcium cation.  Low affinity
interaction of VII and TF is dependent on calcium presence, this affect was reversed by presence of EDTA
in lieu of calcium.
Figure 5: Comparing hydrolysis of peptide in VIIa versus des-(1-38)-VIIa cannot interpret figure, legend
to graph representation not clear.
Figure 6: Analyzing proteolytic activation of fX by VIIa versus des-(1-38)-VIIa Activation of fX appears
higher with TF than truncated TF, though figure legend to graph representation not clear.
Conclusion: Author believes that hypotheses stating multiple interactions systems for the binding of VII
and TF are supported. Myself, not so sure.

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Paper4 fc

  • 1. Kori Jackson Paper 4 Flow Chart 4/7/2014 What Asked: What molecular interactions are integral for the binding of Factor VII to Tissue Factor? How Asked: What molecular (protein-protein) interactions take place in solution and are integral to in solution behavior of Factor VII and it’s binding to VIIa and TF. Which domains are important, and how does Ca2+ affect binding affinity of this system. Figure 1: Analysis of binding tissue factor complesxes with non-inhibitory anti-tissue factor This was to see the TF-VII interaction in solution. Binding of TF complexes to anti-tissue factor not affected by presence of VII. Authors claim that binding of TF complexes to anti-tissue factor reflects concentration of complexes formed in solution. Figure 2: Analysis of factor VII binding to Tissue Factor and extracelluar Tissue Factor domain (TF:1-219)  binding of VII to TF:1-219 had a 10-fold higher Kd than regular TF. Figure 3: Analysis of des-(1-38)-VII binding to TF and TF:1-219. binding was tighter for TF:1-219 than regular TF. Figure 4: Analysis of tissue factor extracellular domain with and without calcium cation.  Low affinity interaction of VII and TF is dependent on calcium presence, this affect was reversed by presence of EDTA in lieu of calcium. Figure 5: Comparing hydrolysis of peptide in VIIa versus des-(1-38)-VIIa cannot interpret figure, legend to graph representation not clear. Figure 6: Analyzing proteolytic activation of fX by VIIa versus des-(1-38)-VIIa Activation of fX appears higher with TF than truncated TF, though figure legend to graph representation not clear. Conclusion: Author believes that hypotheses stating multiple interactions systems for the binding of VII and TF are supported. Myself, not so sure.