Crystal structures of fragments D and double-D from fibrinogen and fibrin

Thrombosis and Haemostasis

Volumn 82, Issue 2, 1999, Pages 271-276

  Doolittle, Russell F ^a   Spraggon, Glen ^b   Everse, Stephen J ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; FIBRIN; FIBRINOGEN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; BETA SHEET; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CONFERENCE PAPER; CRYSTAL STRUCTURE; DISULFIDE BOND; EVOLUTION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; X RAY ANALYSIS;

EID: 0032695014     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615842     Document Type: Conference Paper

References (43)

1. Doolittle RF, Everse SJ, Spraggon G. Human fibrinogen: anticipating a 3-dimensional structure. FASEB J. 1996;10:1464-1470.
2. Yee VC, Pratt KP, Cote HC, LeTrong I, Chung DW, Davie, EW, Stenkamp RE, Teller DC. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure. 1997;5:125-138.
3. Pratt KP, Cote, HCF, Chung DW, Stenkamp RE, Davie EW. The fibrin polymerization pocket: three-dimensional structure of a 30-kDA C-terminal γ chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA. 1997;94:7176-7181.
4. Spraggon G, Everse S, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 1997;389;455-462.
5. Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry. 1998;37:8637-8642.
6. EC domain from human fibrinogen-420. Proc Natl Acad Sci USA. 1998;95:9099-9104.
7. Everse SJ, Spraggon G, Veerapandian L, Doolittle RF. Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide. Biochemistry. 1999;38:2941-2946.
8. Shimizu A, Nagel G, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to γ-chain residues 337-379. Proc Natl Acad Sci USA. 1992;89:2287-2892.
9. Yamazumi K, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to γ-chain Tyr-363. Proc Natl Acad Sci USA. 1992;89:2893-2896.
10. Donahue JP, Patel H, Anderson WF, Hawiger J. Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen γ chain obtained by carrier protein-driven crystallization. Proc Natl Acad Sci USA. 1994;92:12178-12182.
11. Doolittle RF. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Sci. 1992;1: 1563-1577.
12. Williams RC. Morphology of bovine fibrinogen monomers and fibrin oligomers. J Mol Biol. 1981;150:399-408.
13. Weisel JW, Philips GN, Cohen C. A model from electron microscopy for the molecular structure of fibrinogen and fibrin. Nature. 1981;289:263-267.
14. Rao SPS, Poojary D, Elliot BW, Melanson LA, Oriel B, Cohen C. Fibrinogen structure in projection at 18 Å resolution, electron density by co-ordinated cryo-electron microscopy and X-ray crystallography. J Mol Biol. 1991;222:89-98.
15. Weisel JW, Stauffacher CV, Bullitt E, Cohen C. Model for fibrinogen: domains and sequence. Science. 1985;230:1388-1391.
16. Takagi T, Doolittle RF. Amino acid sequence studies on the a chain of human fibrinogen. Location of four plasmin attack points and a covalent cross-linking site. Biochemistry. 1975;14:5149-5156.
17. Doolittle RF, Cassman KG, Cottrell BA, Friezner SJ, Takagi T. Amino acid sequence studies on the α-chain portion of fragment D. Biochemistry. 1977;16:1710-1715.
18. Nieuwenhuizen W. Sites in fibrin involved in the acceleration of plasminogen activation by t-PA. Possible role of fibrin polymerization. Thromb Res. 1994;75:343-347.
19. Laudano AP, Doolittle RF. Synthetic peptide derivatives that bind to fibrinogen and prevent the polymerization of fibrin monomers. Proc Natl Acad Sci USA. 1978;75:3085-3089.
20. Laudano AP, Doolittle RF. Studies on synthetic peptides that bind to fibrinogen and prevent fibrin polymerization. Structural requirements, number of binding sites, and species differences. Biochemistry. 1980;19:1013-1019.
21. Olexa SA, Budzynski A. Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci USA.1980;77:1374-1378.
22. Hasegawa N, Sasaki S. Location of the binding site "b" for lateral polymerization of fibrin. Thromb Res. 1990;57:183-195.
23. Laurent TC, Blomback, B. On the significance of the release of two different peptides from fibrinogen during clotting. Acta Chem Scand. 1958;12:1875-1977.
24. Weisel JW. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 1986;50:1079-1093.
25. Weisel JW, Veklich Y, Gorkun O. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J Mol Biol. 1993;232:285-297.
26. Weisel JW, Warren SG, Cohen C. Crystals of modified fibrinogen: size, shape and packing of molecules. J Mol Biol. 1978;126:159-183.
27. Chen R, Doolittle RF. γ-γ Cross-linking sites in human and bovine fibrin. Biochemistry. 1971;10:4486-4491.
28. Haverkate F, Timan G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments. Thromb Res. 1977;10:803-812.
29. Dang CV, Ebert RF, Bell WR. Localization of a fibrinogen calcium binding site between y-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem. 1985;260:9713-9717.
30. Koopman J, Haverkate F, Briet E, Lord ST. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ chain causing defective calcium binding and impaired fibrin polymerization. J Biol Chem. 1991;266:13456-13461.
31. Matsuda M. The structure-function relationship of hereditary dysfibrinogens. Int J Hematol. 1996;64:167-179.
32. Ebert RF, ed. 1994 Index of variant human fibrinogens. Boca Raton, FL: CRC Press; 1994.
33. Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost. 1998;80:1-9.
34. Cote HCF, Lord ST, Pratt KP. γ-Chain dysfibrinogenemias: molecular structure-functions relationships of naturally occurring mutations in the γ chain of human fibrinogen. Blood. 1998;92:2195-2212.
35. Fellowes AP, Brennan SO, Ridgway HJ, Heaton DC, George PM. Electrospray ionization mass spectrometry identification of fibrinogen Banks Peninsula (gamma280Tyr→Cys): a new variant with defective polymerization. Brit J Haematol. 1998;101:24-31.
36. Doolittle R. The evolution of vertebrate fibrinogen. In: Peeters H, ed. Protides of Biological Fluids. H. Oxford: Pergamon Press; 1980:41-46.
37. Doolittle RF, Spraggon G, Everse SJ. Evolution of vertebrate fibrin formation and the process of its dissolution. In: Bock G, Goode, J, eds. Plasminogen-Related Growth Factors. New York, NY: John Wiley & Sons; 1997:4-17.
38. Selmayr E, Deffner M, Bachmann L, Muller-Berghaus G. Chromatography and electron microscopy of cross-linked fibrin polymers-A new model describing the cross-linking at the DD-trans contact of the fibrin molecules. Biopolymers. 1988; 27:1733-1748.
39. a crosslinked fibrinogen fibrils. J Struct Biol. 1995;115:88-101.
40. Mosesson MW, Siebenlist KR, Meh DA, Wall JS, Hainfeld JF. The location of the carboxy-terminal region of γ chains in fibrinogen and fibrin D domains. Proc Natl Acad Sci USA. 1998;95:10511-10515.
41. Gollwitzer R, Bode W, Karges HE. On the aggregation of fibrinogen molecules. Thromb Res. 1983;(Suppl 5):41-53.
42. Veklich YI, Gorkun OV, Medved LV, Nieuwenhuizen W, Weisel JW. Carboxyl-terminal portions of the α chains of fibrinogen and fibrin. Localization by electron microscopy and the effects of isolated αC fragments on polymerization. J Biol Chem. 1993;268:13577-13585.
43. Gorkun OV, Veklich YI, Medved LV, Henschen AH, Weisel JW. Role of the αC domains of fibrin in clot formation. Biochemistry. 1994; 33:6986-6997.