Sandbox GGC14

Structure

Fibrinogen is located in the circulatory system as part of plasma, it is readily available. Fibrinogen is a ~340KD glycoprotein made up of two subunits which include Aα, Bβ γ. Its central region also called “E region” is where all chains meet, the chains intertwine with each other to hold both of the subunits together. At the ends of the a and b chains are fibrinopeptides, fibrinopeptide A is about 16 amino acids long, while fibrinopeptide B is around 15 amino acids long. These small peptides become very important when activating fibrinogen. On both ends of fibrinogen are the D regions containing the β & γ nodule and the coiled-coil region.

Function

Fibrinogen is an essential protein in coagulation, which is initiated through either an intrinsic or extrinsic pathway. Both pathways trigger a cascade of reactions that lead to the formation of a blood clot. At some point the protease thrombin is activated, thrombin then converts fibrinogen to fibrin. It does this by cleaving both the off of the amino terminus of the alpha and beta chains. The alpha and beta knobs will bind to of other fibrin molecules making fibrin mesh strong enough to hold the platelet plug.

Disease

Congenital Afibrinogenemia – a genetic disorder that results in the lack of fibrinogen which causes abnormal bleeding including gastrointestinal hemorrhage, cutaneous bleeding, etc.

Hepatic fibrinogen storage disease - occurs when there is a mutation in the γ chain which causes the storage of fibrinogen in the ER of liver cells. The storage of fibrinogen in these cells can cause liver disease.

Acquired Dysfibrinogenemia - may occur as a result of liver disease which causes an error during fibrinogen synthesis resulting in dysfunctional fibrinogen

Structural highlights

This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.