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THE STRUCTURE OF FIBRINOGEN AND FIBRIN: II. ARCHITECTURE OF THE FIBRIN CLOT *
Author(s) -
Weisel John W.,
Phillips George N.,
Cohen Carolyn
Publication year - 1983
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1983.tb23257.x
Subject(s) - fibrin , fibrinogen , chemistry , medicine , biochemistry , immunology
Our present low resolution model for fibrinogen based on electron microscopy and x-ray diffraction data has been described by Cohen et al. A unique aspect of the structural analysis of fibrous proteins is that the molecular packing in ordered arrays reflects biologically significant intermolecular interactions. We have shown that the orthogonal sheet microcrystals, which are closely related to fibrin, are made up of a highly regular arrangement of two-stranded protofibrils, and we have visualized aspects of both the substructure of the protofibrils as well as their packing to form the fibrin clot. By correlation of structural data with biochemical studies we have begun to identify certain functional regions of the fibrinogen model related to fibrin. Many aspects of fibrinogen's physiological activity remain to be related to its structure. As our present model is improved by higher resolution studies, we will see with increasing clarity molecular features critical for clot formation and fibrinolysis.