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Thromb Haemost 1999; 82(02): 271-276
DOI: 10.1055/s-0037-1615842
Research Article
Schattauer GmbH

Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

Russell F. Doolittle
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
,
Glen Spraggon
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
,
Stephen J. Everse
1   Center for Molecular Genetics, University of California, San Diego, Novaritis Institute of Functional Genomics, San Diego, CA, USA, and Department of Biochemistry, University of Vermont School of Medicine, Burlington, VT, USA
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Publikationsdatum:
09. Dezember 2017 (online)

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Introduction

After a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved.

* Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

 

  • References

  • 1 Doolittle RF, Everse SJ, Spraggon G. Human fibrinogen: anticipating a 3-dimensional structure. FASEB J. 1996; 10: 1464-1470.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 6 Spraggon G, Applegate D, Everse SJ, Zhang JZ, Veerapandian L, Redman C, Doolittle RF, Grieninger G. Crystal structure of a recombinant extended αEC domain from human fibrinogen-420. Proc Natl Acad Sci USA 1998; 95: 9099-9104.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    PubMedSuche in Google Scholar
  • 11 Doolittle RF. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Sci. 1992; 1: 1563-1577.
    CrossrefPubMedSuche in Google Scholar
  • 12 Williams RC. Morphology of bovine fibrinogen monomers and fibrin oligomers. J Mol Biol. 1981; 150: 399-408.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 15 Weisel JW, Stauffacher CV, Bullitt E, Cohen C. Model for fibrinogen: domains and sequence. Science 1985; 230: 1388-1391.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 22 Hasegawa N, Sasaki S. Location of the binding site “b” for lateral polymerization of fibrin. Thromb Res. 1990; 57: 183-195.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 24 Weisel JW. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 1986; 50: 1079-1093.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 26 Weisel JW, Warren SG, Cohen C. Crystals of modified fibrinogen: size, shape and packing of molecules. J Mol Biol. 1978; 126: 159-183.
    CrossrefPubMedSuche in Google Scholar
  • 27 Chen R, Doolittle RF. γ-γ Cross-linking sites in human and bovine fibrin. Biochemistry. 1971; 10: 4486-4491.
    CrossrefPubMedSuche in Google Scholar
  • 28 Haverkate F, Timan G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments. Thromb Res. 1977; 10: 803-812.
    CrossrefPubMedSuche in Google Scholar
  • 29 Dang CV, Ebert RF, Bell WR. Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem. 1985; 260: 9713-9717.
    PubMedSuche in Google Scholar
  • 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.
    PubMedSuche in Google Scholar
  • 31 Matsuda M. The structure-function relationship of hereditary dysfibrinogens. Int J Hematol. 1996; 64: 167-179.
    CrossrefPubMedSuche in Google Scholar
  • 32 Ebert RF. ed. 1994 Index of variant human fibrinogens. Boca Raton, FL: CRC Press; 1994
    Suche in Google Scholar
  • 33 Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost. 1998; 80: 1-9.
    Thieme ConnectPubMedSuche in Google Scholar
  • 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.
    PubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 36 Doolittle R. The evolution of vertebrate fibrinogen. In: Peeters H. ed. Protides of Biological Fluids. H. Oxford: Pergamon Press; 1980: 41-46.
    Suche in Google Scholar
  • 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.
    Suche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 39 Mosesson MW, Siebenlist KR, Hainfeld JF, Wall JS. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. J Struct Biol. 1995; 115: 88-101.
    CrossrefPubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar
  • 41 Gollwitzer R, Bode W, Karges HE. On the aggregation of fibrinogen molecules. Thromb Res. 1983; (Suppl. 05) 41-53.
    PubMedSuche in Google Scholar
  • 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.
    PubMedSuche in Google Scholar
  • 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.
    CrossrefPubMedSuche in Google Scholar