Homology models of the C domains of blood coagulation factors V and VIII: A proposed membrane binding mode for FV and FVIII C2 domains

Blood Cells, Molecules, and Diseases

Volumn 24, Issue 4, 1998, Pages 448-461

  Pellequer, Jean Luc ^a   Gale, Andrew J ^a   Griffin, John H ^a   Getzoff, Elizabeth D ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Blood coagulation; Factor V; Factor VIII; Membrane; Modeling; Phospholipid; Thrombosis

Indexed keywords

BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 5A; BLOOD CLOTTING FACTOR 8; GALACTOSE OXIDASE; PROTEIN SUBUNIT;

AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; BLOOD CLOTTING; MEMBRANE BINDING; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; STEREOCHEMISTRY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS;

EID: 0032467348     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1006/bcmd.1998.0214     Document Type: Article

References (66)

1. 1. Mann KG, Nesheim ME, Hibbard LS, Tracy PB. The role of factor V in the assembly of the prothrombinase complex, in Walz DA, McCoy LE (eds): Annals of the New York Academy of Sciences. New York, New York Academy of Sciences, pp. 378-388, 1981.
2. 2. Tracy PB, Mann KG. Prothrombinase complex assembly on the platelet surface is mediated through the 74,000-dalton component of factor Va. Proc Natl Acad Sci USA 80:2380-2384, 1983.
3. 3. Krishnaswamy S, Church WR, Nesheim ME, Mann KG. Activation of human prothrombin by human prothrombinase: Influence of factor Va on the reaction mechanism. J Biol Chem 262:3291-3299, 1987.
4. 4. Rosing J, Tans G, Govers-Riemslag JWP, Zwaal RFA, Hemker HC. The role of phospholipids and factor Va in the prothrombinase complex. J Biol Chem 255:274-283, 1980.
5. 5. Esmon CT. The subunit structure of thrombin-activated factor V: Isolation of activated factor V, separation of subunits, and reconstitution of biological activity. J Biol Chem 254:964-973, 1979.
6. 6. Kane WH, Davie EW. Blood coagulation factors V and VIII: Structure and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood 71:539-555, 1988.
7. 7. Dählback B. Human coagluation factor V purification and thrombin-catalyzed activation. J Clin Invest 66:583-591, 1980.
8. 8. Nesheim ME, Myrmel KH, Hibbard L, Mann KG. Isolation and characterization of single chain bovine factor V J. Biol Chem 254:508-517, 1979.
9. 9. Kane WH, Majerus PW. Purification and characterization of human coagulation factor V. J Biol Chem 256:1002-1007, 1981.
10. 10. Jenny RJ, Pittman DD, Toole JJ, et al. Complete cDNA and derived amino acid sequence of human factor V. Proc Natl Acad Sci USA 84:4846-4850, 1987.
11. 11. Suzuki K, Dählbeck B, Stenflo JA. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem 257:6556-6564, 1982.
12. 12. van Dieijen G, Tans G, Rosing J, Hemker HC. The role of phospholipid and factor VIIIa in the activation of bovine factor X. J Biol Chem 256:3433-3442, 1981.
13. 13. Pan Y, DeFay T, Gitschier J, Cohen FE. Proposed structure of the A domains of factor VIII by homology modelling. Nature Struct Biol 2:740-744, 1995.
14. 14. Pemberton S, Lindley P, Zaitsev V, Card G, Tuddenham EGD, Kemball-Cook G. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 89:2413-2421, 1997.
15. 15. Pellequer J-L, Gale AJ, Griffin JH, Getzoff ED. Homology modeling of Factor Va, a cofactor of the prothrombinase complex. Protein Sci 7(suppl 1):159, 1998.
16. 16. Villoutreix BO, Dählback B. Structural investigation of the A domains of human blood coagulation factor V by molecular modeling. Protein Sci 7:1317-1325, 1998.
17. 17. Zaitseva I, Zaitsev V, Card G, et al. The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres. J Biol Inorg Chem 1:15-23, 1996.
18. 18. Kane WH, Davie EW. Cloning of a cDNA coding for human factor V, a blood coagulation factor homologous to factor VIII and ceruloplasmin. Proc Natl Acad Sci USA 83:6800-6804, 1986.
19. 19. Poole S, Firtel RA, Lamar E, Rowekamp W. Sequence and expression of the discoidin I gene family in Dictyostelium discoideum. J Mol Biol 153:273-289, 1981.
20. 20. Baumgartner S, Hofmann K, Chiquet-Ehrismann R, Bucher P. The discoidin domain family revisited: New members from prokaryotes and a homology-based fold prediction. Protein Sci 7:1626-1631, 1998.
21. 21. Ortel TL, Devore-Carter D, Quinn-Allen MA, Kane WH. Deletion analysis of recombinant human factor V. Evidence for a phosphatidylserine binding site in the second C-type domain. J Biol Chem 267:4189-4198, 1992.
22. 22. Ortel TL, Quinn-Allen MA, Keller FG, Peterson JA, Larocca D, Kane WH. Localization of functionally important epitopes within the second C-type domain of coagulation factor V using recombinant chimeras. J Biol Chem 269:15898-15905, 1994.
23. 23. Kalafatis M, Jenny RJ, Mann KG. Identification and characterization of a phospholipid-binding site of bovine factor Va. J Biol Chem 265:21580-21589, 1990.
24. 24. Kalafatis M, Rand MD, Mann KG. Factor Va-membrane interaction is mediated by two regions located on the light chain of the cofactor. Biochemistry 33:486-493, 1994.
25. 25. Krishnaswamy S, Mann KG. The binding of factor Va to phospholipid vesicles. J Biol Chem 263:5714-5723, 1988.
26. 26. Bloom JW, Nesheim ME, Mann KG. Phospholipid-binding properties of bovine factor V and factor Va. Biochemistry 18:4419-4425, 1979.
27. 27. Pusey ML, Mayer LD, Wei GJ, Bloomfield VA, Nelsestuen GL. Kinetic and hydrodynamic analysis of blood clotting factor V-membrane binding. Biochemistry 21:5262-5269, 1982.
28. 28. Cutsforth GA, Koppaka V, Krishnaswamy S, Wu JR, Mann KG, Lentz BR. Insights into the complex association of bovine factor Va with acidic-lipid-containing synthetic membranes. Biophys J 70:2938-2949, 1996.
29. 29. Lecompte MF, Bouix G, Mann KG. Electrostatic and hydrophobic interactions are involved in factor Va binding to membranes containing acidic phospholipids. J Biol Chem 269:1905-1910, 1994.
30. 30. Ito N, Phillips SEV, Yadav KDS, Knowles PF. Crystal structure of a free radical enzyme, galactose oxidase. J Mol Biol 238:794-814, 1994.
31. 31. Fischer D, Eisenberg D. Fold recognition using sequence-derived predictions. Protein Sci 5:947-955, 1996.
32. 32. Rost B, Sander C. Prediction of protein structure at better than 70 % accuracy. J Mol Biol 232:584-599, 1993.
33. 33. Rost B, Sander C, Schneider R. PHD - an automatic mail server for protein secondary structure prediction. Comput Applic Biosci 10:53-60, 1994.
34. 34. Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637, 1983.
35. 35. Devereux J, Haeberli P, Smithies O. A comprehensive set of sequence analyses program for the VAX. Nucl Acid Res 12:387-395, 1984.
36. 36. McRee DE. XtalView: A visual protein crystallographic software system for X11/XView. J Mol Graph 10:44-47, 1992.
37. 37. Tuffery P, Etchebest C, Hazout S, Lavery R. A new approach to the rapid determination of protein side chain conformations. J Biomol Struct Dynam 8:1267-1289, 1991.
38. 38. Brünger AT. X-PLOR Manual. Version 3.0. New Haven, Yale University, 1992.
39. 39. Brooks B, Bruccoleri R, Olafson B, States D, Swaminathan S, Karplus M. CHARMM: A program for macromolecular energy, minimization, and molecular dynamics calculations. J Comp Chem 4:187-217, 1983.
40. 40. Brünger AT, Karplus M. Polar hydrogen positions in proteins: empirical energy function placement and neutron diffraction comparison. Proteins 4:148-156, 1988.
41. 41. Powell MJD. Restart procedures for the conjugate gradient method. Math Program 12:241-254, 1977.
42. 42. Roussel A, Cambillau C. TURBO-FRODO: Silicon Graphics geometry partners directory. Mountain View, California, Silicon Graphics, pp. 77-78, 1989.
43. 43. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Cryst 26:283-291, 1993.
44. 44. Rosing J, Bakker HM, Thomassen MCLGD, Hemker HC, Tans G. Characterization of two forms of human factor Va with different cofactor activities. J Biol Chem 268:21130-21136, 1993.
45. 45. Ortel TL, Yoo L, Quinn-Allen MA, Kane WH. Partial glycosylation at asparagine-2181 of the second C-type domain of human factor V is the structural basis of the light chain doublet. Blood 84(suppl 1):387A, 1994.
46. 46. Chothia C. Hydrophobic bonding and accessible surface area in proteins. Nature 248:338-339, 1974.
47. 47. Stoylova S, Mann KG, Brisson A. Structure of membrane-bound human factor Va. FEBS Lett 351:330-334, 1994.
48. 48. Arai M, Scandella D, Hoyer LW. Molecular basis of factor VIII inhibition by human antibodies. Antibodies that bind to the factor VIII light chain prevent the interaction of factor VIII with phospholipid. J Clin Invest 83:1978-1984, 1989.
49. 49. Foster PA, Fulcher CA, Houghten RA, Zimmerman TS. Synthetic factor VIII peptides with amino acid sequences contained with the C2 domain of factor VIII inhibit factor VIII binding to phosphatidylserine. Blood 75:1999-2004, 1990.
50. 50. Kim J, Mosior M, Chung LA, Wu H, McLaughlin S. Binding of petides with basic residues to membranes containing acidic phospholipids. Biophys J 60:135-148, 1991.
51. 51. Denisov G, Wanaski S, Luan P, Glaser M, McLaughlin S. Binding of basic peptides to membranes produces lateral domains enriched in the acidic lipids phosphatidylserine and phosphatidylinositol 4,5-biphosphate: An electrostatic model and experimental results. Biophys J 74:731-744, 1998.
52. 52. Yang L, Glaser M. Membrane domains containing phosphatidylserine and substrate can be important for the activation of protein kinase C. Biochemistry 34: 1500-1506, 1995.
53. 53. Glaser M, Wanaski S, Buser CA, et al. Reversible inhibition of phospholipase C by sequestration of phosphatidylinositol 4,5-bisphosphate in lateral domains. J Biol Chem 271:26187-26193, 1996.
54. 54. Qin Z, Cafiso DS. Membrane structure of protein kinase C and calmodulin binding domain of Myristoylated Alanine Rich C Kinase Substrate determined by site-directed spin labeling. Biochemistry 35:2917-2925, 1996.
55. 55. Krieg UC, Isaacs BS, Yemul SS, Esmon CT, Bayley H, Johnson AE. Interaction of blood coagulation factor Va with phospholipid vesicles examined by using lipophilic photoreagents. Biochemistry 26:103-109, 1987.
56. 56. Lecompte M-F, Krishnaswamy S, Mann KG, Nesheim ME, Gitler C. Membrane penetration of bovine factor V and Va detected by labeling with 5-iodonaphthalene-1-azide. J Biol Chem 262:1935-1937, 1987.
57. 57. Mayer LD, Pusey ML, Griep MA, Nelsestuen GL. Association of blood coagulation factors V and X with phospholipid monolayers. Biochemistry 22:6226-6232, 1983.
58. 58. Nilsson I, von Heijne G. Fine-tuning the topology of a polytopic membrane protein: Role of positively and negatively charged amino acids. Cell 62:1135-1141, 1990.
59. 59. Pusey ML, Nelsestuen GL. Membrane binding properties of blood coagulation Factor V and derived peptides. Biochemistry 23:6202-6210, 1984.
60. 60. Bloom JW. The interaction of rDNA factor VIII, factor VIIIdes-797-1562 and factor VIIIdes-797-1562-derived peptides with phospholipid. Thromb Res 48:439-448, 1987.
61. 61. Gilbert GE, Furie BC, Furie B. Binding of human factor VIII to phospholipid vesicles. J Biol Chem 265:815-822, 1990.
62. 62. Gilbert GE, Baleja JD. Membrane-binding peptide from the C2 domain of factor VIII forms an amphipathic structure as determined by NMR spectroscopy. Biochemistry 34:3022-3031, 1995.
63. 63. Veeraraghavan S, Baleja JD, Gilbert GE. Structure and topography of the membrane-binding C2 domain of factor VIII in the presence of dodecylphosphocholine micelles. Biochem J 332:549-555, 1998.
64. 64. Kraulis PJ. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J Appl Cryst 24:946-950, 1991.
65. 65. Bacon DJ, Anderson WF. A fast algorithm for rendering space-filling molecule pictures. J Mol Graph 6:219-220, 1988.
66. 66. Merritt EA, Murphy MEP. Raster3D version 2.0, a program for photorealistic molecular graphics. Acta Cryst D50:869-873, 1994.