fibrinogen complex

Definition

Target type: cellularcomponent

A highly soluble, elongated protein complex found in blood plasma and involved in clot formation. It is converted into fibrin monomer by the action of thrombin. In the mouse, fibrinogen is a hexamer, 46 nm long and 9 nm maximal diameter, containing two sets of nonidentical chains (alpha, beta, and gamma) linked together by disulfide bonds. [ISBN:0198547684]

Fibrinogen complex is a multimeric protein complex composed of six polypeptide chains: two Aα chains, two Bβ chains, and two γ chains. These chains are arranged in a symmetrical trimeric structure, with each monomer consisting of three globular domains, designated as D, E, and A (or B) for the α, β, and γ chains, respectively. The D domains are located at the N-terminus of the chains and are responsible for the formation of the fibrinogen molecule. The E domains are central and facilitate the assembly of the trimeric structure. The A and B domains are located at the C-terminus and are involved in fibrin polymerization.

The D domains of the α, β, and γ chains interact with each other through noncovalent interactions to form a central core structure. This core structure is responsible for the overall stability of the fibrinogen molecule.

The E domains are located on either side of the central core structure. These domains are involved in the formation of the trimeric structure of fibrinogen and are also essential for the interaction of fibrinogen with other proteins, such as the fibrinolytic enzymes plasminogen and plasmin.

The A and B domains are located at the ends of the fibrinogen molecule and are involved in the polymerization of fibrin monomers into a fibrin clot. The A domains are located at the C-terminus of the α chains and are responsible for the formation of the fibrin clot. The B domains are located at the C-terminus of the β chains and are involved in the interaction of fibrinogen with other proteins, such as the coagulation factor XIII.

In summary, the cellular component of fibrinogen complex consists of a symmetrical trimeric structure, with each monomer consisting of three globular domains, designated as D, E, and A (or B) for the α, β, and γ chains, respectively. The D domains are responsible for the formation of the fibrinogen molecule, the E domains facilitate the assembly of the trimeric structure, and the A and B domains are involved in fibrin polymerization.'
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Proteins (1)

Compounds (1)