Fibrinogen structure

Lucas M. A., Fretto L. S., McKee P. A. The relationship of fibrinogen structure to plasminogen activation and plasmin activity during fibrinolysis. Ann N Y Acad Sci 1983 408, 71-91. 

Hantgan, R. R., Simpson-Haidaris, P. J., Francis, C. W., and Marder, V. J. (2000). Fibrinogen structure and physiology. In Hemostasis and Thrombosis Basic Principles and Clinical Practice (R. W. Colman, J. Hirsh, V. J. Marder, A. W. Clowes, andj. N. George, Eds.), pp. 203-232. Lippincott, Williams Wilkins, Philadelphia. 

Rao, S., Poojary, M., Elliott, B., Melanson, L., Oriel, B., and Cohen, C. (1991). Fibrinogen structure in projection at 18 A resolution. Electron density by co-ordinated cryo-electron microscopy and X-ray crystallography. J. Mol. Biol. 222, 89-98. 

Hawiger J, Kloczewiak M, Bednardc MA, Timmons S. Platelet receptor recognition domains on the a diain of human fibrinogen Structure-function analysis. Biochemistry 1989 28 2909-2914. 

M. W. Mosesson Fibrinogen structure and fibrin clot a.ssembly. Seminars in Thrombosis and Hemostasis 24, 169 (1998). 

Wnek, G.E., et al., 2003. Electrospinning of nanofiber fibrinogen structures. Nano Letters 3 (2),... 

Alpha helices are sufficiently versatile to produce many very different classes of structures. In membrane-bound proteins, the regions inside the membranes are frequently a helices whose surfaces are covered by hydrophobic side chains suitable for the hydrophobic environment inside the membranes. Membrane-bound proteins are described in Chapter 12. Alpha helices are also frequently used to produce structural and motile proteins with various different properties and functions. These can be typical fibrous proteins such as keratin, which is present in skin, hair, and feathers, or parts of the cellular machinery such as fibrinogen or the muscle proteins myosin and dystrophin. These a-helical proteins will be discussed in Chapter 14. 

Spraggon, G., et al. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 389 455-462, 1997. 

The hydantoin moiety has been utilized as a biostere for the peptide linkage, transforming a peptide lead into an orally available drug candidate. Therefore, an Arg-Gly-Asp-Ser tetrapeptide (18) lead structure was modified to a non-peptide RGD mimetic as an orally active fibrinogen receptor antagonist 19. ° ... 

Fibrinolytics. Figure 2 Various fibrin structures for plasmin. Fibrinogen (Fg) is converted to fibrin (F) by thrombin (T), and thrombin can also convert factor XIII (XIII) to activated factor XIII (Xllla). The latter produces crosslinks between fibrins (FxxF) and also may crosslink fibrin with a2-plasmin inhibitor (FxxFxxPI). The efficiency of digestion of these plasmin substrates by plasmin, resulting in the soluble fibrin degradation products (FDP), is different. The amount of FDP formed in time is expressed in arbitrary units. 

A 3D model of the fibrinogen-derived (very late antigen-4, VLA-4) inhibitor 4-[N -(2-methylphenyl)ureido]phenylacetyl-Leu-Asp-Val was derived from the X-ray structure of the related integrin-binding region of the vascular cell adhesion molecule-1 (VCAM-1). A 3D pharmacophore was generated with the program Catalyst, and a 3D search was performed in 8624 molecules from... 

I Fibrinogen Both Forms structural basis of clot after its conversion to fibrin... 

Fibrinogen (factor I) is a large (340 kDa) glycoprotein consisting of two identical tri-polypeptide units, a, P and y. Its overall structural composition may thus be represented as (a P y)2. 

---