Structure of membrane-bound human factor Va

Svetla Stoylova, Kenneth G. Mann, Alain Brisson

Research output: Contribution to journalArticlepeer-review

34 Scopus citations


Coagulation factor Va is an essential cofactor which combines with the serine protease factor Xa on a phospholipid surface to form the prothrombinase complex. In the present study, the structure of factor Va interacting with lipid surfaces containing phosphatidylserine was studied by electron microscopy. Two-dimensional crystals of factor Va were obtained on planar lipid films under quasi-physiological conditions. The two-dimensional projected structure of factor Va was calculated at a resolution of 2 nm, revealing dimers of factor Va arranged on the surface lattice with the symmetry of the plane group p2. Average unit cell dimensions are a = 14.4 nm, b = 8.8 nm, γ = 107°. Each factor Va molecule presents two distinct domains of protein density consisting of one small domain, of 3 nm in diameter, connected to a larger domain of about 6 nm × 4.5 nm. The projected structure of factor Va covers an area equivalent to about fifty phospholipid molecules. In addition, edge-on views of factor Va molecules bound to liposomes reveal a globular structure connected through a thin stem to the liposome surface. A three-dimensional model of membrane-bound factor Va is proposed.

Original languageEnglish (US)
Pages (from-to)330-334
Number of pages5
JournalFEBS Letters
Issue number3
StatePublished - Sep 12 1994
Externally publishedYes


  • Electron microscopy
  • Factor Va
  • Liposome
  • Phosphatidylserine
  • Two-dimensional crystal

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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