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Structure of membrane-bound human factor Va

S Stoylova1, K G Mann, A Brisson

  • 1Laboratoire de Génétique Moléculaire des Eucaryotes, CNRS, Unité 184 de Biologie Moléculaire et de Génie Génétique, INSERM, Faculté de Médecine, Strasburg, France.

FEBS Letters
|September 12, 1994
PubMed
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This study reveals the structure of coagulation factor Va (FVa) bound to lipid surfaces using electron microscopy. The findings show FVa forms dimers with distinct domains, offering insights into the prothrombinase complex formation.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Hematology

Background:

  • Coagulation factor Va (FVa) is a critical cofactor in blood coagulation.
  • FVa, along with factor Xa, forms the prothrombinase complex on phospholipid surfaces.
  • Understanding FVa's interaction with lipids is key to comprehending hemostasis.

Purpose of the Study:

  • To elucidate the structural organization of factor Va when interacting with phosphatidylserine-containing lipid surfaces.
  • To provide a detailed structural model of membrane-bound factor Va.

Main Methods:

  • Electron microscopy was employed to study factor Va structure.
  • Two-dimensional crystallization of factor Va on planar lipid films under quasi-physiological conditions.
  • Calculation of the two-dimensional projected structure at 2 nm resolution.

Related Experiment Videos

Main Results:

  • Factor Va forms dimers arranged in a p2 plane group lattice on lipid surfaces.
  • Each factor Va molecule exhibits two domains: a small (3 nm diameter) and a larger (6 nm x 4.5 nm) domain.
  • Edge-on views show a globular structure connected by a stem to liposomes, forming a proposed 3D model of membrane-bound FVa.

Conclusions:

  • The study provides high-resolution structural insights into membrane-bound factor Va.
  • The proposed model aids in understanding the assembly and function of the prothrombinase complex.
  • These findings contribute to the structural knowledge of key hemostatic factors.