Ukr.Biochem.J. 2020; Volume 92, Issue 3, May-Jun, pp. 22-32


Structure and function of fibrinogen BβN-domains

L. Medved*, S. Yakovlev

Center for Vascular and Inflammatory Diseases and Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD, USA;

Received: 17 May 2020; Accepted: 30 June 2020

Fibrinogen is a polyfunctional plasma protein involved in various physiological and pathological processes through the interaction of its multiple domains with different ligands and cell receptors. Among fibrinogen domains, two BβN-domains are formed by the N-terminal portions of its two Bβ chains including­ amino acid residues Bβ1-64. Although their folding status is not well understood and the recombinant disulfide-linked (Bβ1-66)2  fragment corresponding to a pair of these domains was found to be unfolded, some data suggest that these domains may be folded in the parent molecule. In contrast, their major functional properties are well established. Removal of fibrinopeptides B (amino acid residues Bβ1-14) from these domains upon fibrinogen to fibrin conversion results in the exposure of multiple binding sites in fibrin βN-domains (residues β15-64). These sites provide interaction of the βN-domains with different proteins and cells and their participation in various processes including fibrin assembly, fibrin-dependent angiogenesis, and fibrin-dependent leukocyte transmigration and thereby inflammation. The objective of this review is to summarize the current view of the structure and function of these domains in fibrinogen and fibrin and their role in the above-mentioned processes.

Keywords: , , , ,


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