Cryo-electron microscopy of coagulation Factor VIII bound to lipid nanotubes

Biochemical and Biophysical Research Communications

Volumn 366, Issue 2, 2008, Pages 288-293

  Parmenter, Christopher D J ^a   Cane, Matthew C ^a   Zhang, Rui ^b   Stoilova McPhie, Svetla ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

^b BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

Coagulation Factor VIII; Cryo electron microscopy; Image analysis; Lipid nanotubes; Membrane binding; Models fitting

Indexed keywords

BLOOD CLOTTING FACTOR 8; LIPID; NANOTUBE;

ARTICLE; BINDING AFFINITY; CRYOELECTRON MICROSCOPY; DENSITY; HYDROPHOBICITY; IMAGE ANALYSIS; LIPID BILAYER; MEMBRANE BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; THICKNESS;

BINDING SITES; COMPUTER SIMULATION; CRYOELECTRON MICROSCOPY; FACTOR VIII; LIPID BILAYERS; MODELS, CHEMICAL; MODELS, MOLECULAR; NANOTUBES; PROTEIN BINDING; PROTEIN CONFORMATION;

EID: 37449003239     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.11.072     Document Type: Article

References (24)

1. Kemball-Cook G., Tuddenham E.G.D., and Wacey A.I. The factor VIII structure and mutation resource site: HAMSTeRS version. Nucleic Acids Res. 26 (1998) 216-219
2. Tuddenham E.G.D. Factor VIII-novel insights into form and function. Br. J. Haematol. 119 (2002) 232-331
3. Jankowski M.A., Patel H., Rouse J.C., Marzilli L.A., Weston S.B., and Sahrpe P.J. Defining 'full-length' recombinant factor VIII: a comparative structural analysis. Haemophilia 13 (2007) 30-37
4. Sandberg H., Almsteadt A., Brandt J., Gray E., Holmquist L., Oswaldsson U., Sebring S., and Mikaelsson M. Structural and functional characteristics of the B-domain deleted recombinant factor VIII protein, r-VIII SQ. Thromb. Haemost. 85 (2001) 93-100
5. Gilbert G.E., Furie B.C., and Furie B. Binding of human factor VIII to phospholipid vesicles. J Biol. Chem. 265 (1990) 815-822
6. van Dieijen G., Tans G., Rosing J., and Hemker H.C. The role of phsopholipids and factor VIIIa in the activation of bovine factor 10. J. Biol. Chem. 256 (1981) 3433-3442
7. Wood W.I., Capon D.J., Simonsen C.C., Eaton D.L., Gitschier J., Keyt B., Seeburg P.H., Smith D.H., Hollingshead P., Wion K.L., Delwart E., Tuddenham E.G.D., Vehar G.A., and Lawn R.M. Expression of active human factor VIII from recombinant DNA clones. Nature 312 (1984) 330-337
8. Pemberton S., Lindley P., Zaitsev V., Card G., Tuddenham E.G.D., and Kemball-Cook G. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 89 (1997) 2413-2421
9. Pratt P., Shen B.W., Takashima K., Devie E.W., Fujikawa K., and Stoddard B.L. Structure of the C2 domain of human factor VIII at 1.5 Ǻ. Nature 402 (1999) 422-439
10. Liu M.L., Shen B.W., Nakaya S., Pratt K.P., Fujikawa K., Devie E.W., Stoddard B.L., and Thompson A.R. Hemophilic factor VIII C1- and C2-domain missense mutations and their modelling to the 1.5-angstrom human C2-domain crystal structure. Blood 30 (2000) 979-987
11. Fay P.J. Activation of factor VIII and mechanism of cofactor action. Blood rev. 18 (2004) 1-15
12. Fay P.J., Haidaris P.J., and Smudzin T.M. Human factor VIII subunit structure. J. Biol. Chem. 266 (1991) 8957-8962
13. Wilson-Kubalek E.M. Preparation of functionalized lipid tubules for electron crystallography of macromolecules. Methods Enzymol. 312 (2000) 515-519
14. Wilson-Kubalek E.M., Brown R.E., Celia H., and Milligan R.A. Lipid nanotubes as substrates for helical crystallization of macromolecules. Proc. Natl. Acad. Sci. USA 95 (1998) 8040-8045
15. Egelman E.H. Single-particle reconstruction from EM images of helical filaments. Curr. Opin. Str. Biol. 17 (2007) 1-6
16. Dang T.X., MIlligan R.A., Tweten R.K., and Wilson-Kubalek E.M. Helical crystallization on nickel-lipid nanotubes: perfringolysin O as a model protein. J. Struct. Biol. 152 (2005) 129-139
17. Dang T.X., Farah S.J., Gast A., Robertson C., Carragher B., Egelman E., and Wilson-Kubalek E.M. Helical crystallization on lipid nanotubes: streptavidin as a model protein. J. Struct. Biol. 150 (2005) 90-99
18. Stoilova-McPhie S., Villoutreix B.O., Mertens K., Kembal-Cook G., and Holzenburg A. 3-Dimensional structure of membrane-bound coagulation factor VIII: modeling of the factor VIII heterodimer within a 3-dimensional density map derived by electron crystallography. Blood 99 (2002) 1215-1223
19. Autin L., Miteva M.A., Lee W.H., Mertens K., Radtke K.-P., and Villoutreix B.O. Molecular models of the procoagulant Factor VIIIa-Factor IXa complex. J. Thromb. Haemost. 3 (2005) 2044-2056
20. S. Stoilova-McPhie, C.D.J. Parmenter, K. Segers, B.O. Villoutreix, G.A.F. Nicolaes, Defining the structure of membrane-bound human blood coagulation Factor Va, J. Thromb. Haemost., in Press.
21. Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
22. Pettersen E.F., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., and Ferrin T.E. UCSF Chimera-A visualization system for exploratory research and analysis. J. Comput. Chem. 25 (2004) 1605-1612
23. Parmenter C., and Stoilova-McPhie S. Cryo-electron mciroscopy of phospholipid vesicles with bound coagulation factor VIII. Microsc. Anal. 21 6 (2007) S9-S11
24. Adams T.E., Hockin M.F., Mann K.G., and Everse S.J. The crystal structure of activated protein C-inactivated bovine factor Va: implications for cofactor function. Proc. Natl. Acad. Sci. USA 101 (2004) 8918-8923