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Phosphatidylserine and FVa regulate FXa structure.

Kinshuk Raj Srivasatava1, Rinku Majumder1, William H Kane2

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PubMed
Summary
This summary is machine-generated.

This study reveals how phosphatidylserine (PS) binding alters Factor Xa (FXa) structure, impacting blood coagulation. FRET measurements show FXa undergoes significant length changes upon binding to PS and its cofactor Factor Va (FVa), explaining its allosteric regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Human coagulation Factor Xa (FXa) is crucial for blood clotting, activating prothrombin to thrombin on platelet membranes.
  • Phosphatidylserine (PS) exposure on activated platelets allosterically regulates FXa, enhancing prothrombin activation.
  • The structural basis for PS-mediated allosteric regulation of FXa remains incompletely understood.

Purpose of the Study:

  • To elucidate the structural changes in FXa induced by phosphatidylserine (PS) and its cofactor Factor Va (FVa).
  • To identify the molecular sites and mechanisms involved in FXa allosteric regulation by PS.
  • To assess the utility of Förster Resonance Energy Transfer (FRET) in studying FXa structure-function relationships.

Main Methods:

  • Utilized Förster Resonance Energy Transfer (FRET) to monitor conformational changes (length) in FXa.
  • Investigated FXa structural responses to soluble short-chain PS (C6PS), PS-containing membranes, and FVa.
  • Employed a FRET pair with a donor at the FXa active site and an acceptor at the N-terminus.

Main Results:

  • FXa structure changes upon binding to C6PS at both an N-terminal regulatory site and a catalytic domain site.
  • Binding of C6PS increased FXa interprobe distance by ~3 Å, with saturation of both sites increasing it by ~6.4 Å.
  • FXa binding to membranes caused a smaller length increase (~1.4 Å), but combined with FVa2, the total change (~5.6-5.8 Å) was comparable to C6PS regulation.

Conclusions:

  • FXa undergoes distinct structural alterations upon binding to PS and FVa, explaining its allosteric regulation.
  • The functional regulation of FXa by C6PS or membranes in conjunction with FVa2 correlates with similar structural changes.
  • FRET is a valuable technique for analyzing structure-function relationships in FXa and its complexes.