Is a major plasma glycoprotein (350 kDa) that plays an important role in blood clotting, cellular and matrix interactions, inflammation, wound healing, and neoplasia.
Fibrinogen is a 340 kDa glycoprotein that consists of two identical disulfide-linked subunits. Each subunit is composed of three nonidentical polypeptide chains: alpha, beta, and gamma. The beta and gamma chains have conserved C-terminal domains of about 250 amino acid residues (designated βC and γC, respectively). The crystal structure of the isolated γC domain, as well as that of the γC and βC domains in the fibrinogen D fragment, revealed that both domains are similarly folded. A minor 420 kDa form of fibrinogen (fibrinogen-420) has an alternative extended form of the alpha chain (αE), which has a C-terminal domain (designated αEC) whose sequence and fold are highly homologous to those of the βC and γC domains. Fibrinogen binds to CD54 (ICAM-1) through the first IgG domain (8KVILPRGGSVLVTC21...