Factor Va alternative conformation reconstruction using atomic force microscopy

Journal: Thrombosis and Haemostasis
ISSN: 0340-6245
Issue: 2014: 112/6 (Dec) pp. 1077–1327
Pages: 1167-1173
Ahead of Print: 2014-09-04

Factor Va alternative conformation reconstruction using atomic force microscopy

Online Supplementary Material

R. C. Chaves (1), S. Dahmane (1, 2), M. Odorico (1), G. A. F. Nicolaes (3), J.-L. Pellequer (1, 4)

(1) CEA, iBEB, Service de Biochimie et Toxicologie Nucléaire, Bagnols sur Cèze, France; (2) Present address: Inserm, Unité 1054, Single Molecule Biophysics Department, Centre de Biochimie Structurale, Montpellier, France; (3) Department of Biochemistry, Cardiovascular Research Institute Maastricht, CARIM, Maastricht University, the Netherlands; (4) New address: IBS, Univ. Grenoble Alpes/CNRS/CEA, 71 avenue des Martyrs CS 10090, F-38044 Grenoble, Cedex 9, France


imaging, Coagulation factors, phospholipids, atomic force microscopy, protein structure / folding


Protein conformational variability (or dynamics) for large macromolecules and its implication for their biological function attracts more and more attention. Collective motions of domains increase the ability of a protein to bind to partner molecules. Using atomic force microscopy (AFM) topographic images, it is possible to take snapshots of large multi-component macromolecules at the single molecule level and to reconstruct complete molecular conformations. Here, we report the application of a reconstruction protocol, named AFM-assembly, to characterise the conformational variability of the two C domains of human coagulation factor Va (FVa). Using AFM topographic surfaces obtained in liquid environment, it is shown that the angle between C1 and C2 domains of FVa can vary between 40° and 166°. Such dynamical variation in C1 and C2 domain arrangement may have important implications regarding the binding of FVa to phospholipid membranes.

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