Plasmin-α2-antiplasmin

Plasmin-α2-antiplasmin is a complex formed by the binding of plasmin, a serine protease, and α2-antiplasmin, a serpin superfamily protein. This complex plays a crucial role in the regulation of fibrinolysis, the process that prevents blood clots from growing and becoming problematic.

Function

The primary function of the plasmin-α2-antiplasmin complex is to inhibit the activity of plasmin. Plasmin is an enzyme that breaks down fibrin, a protein that is a major component of blood clots. By inhibiting plasmin, the plasmin-α2-antiplasmin complex helps to control the size of blood clots and prevent excessive bleeding.

Structure

The plasmin-α2-antiplasmin complex is formed when α2-antiplasmin binds to the active site of plasmin. This binding changes the shape of the plasmin molecule, rendering it unable to break down fibrin.

Clinical significance

Abnormalities in the plasmin-α2-antiplasmin complex can lead to a variety of health problems. For example, a deficiency in α2-antiplasmin can result in excessive bleeding, while an overabundance of this protein can lead to the formation of abnormal blood clots. Additionally, certain mutations in the genes that encode for plasmin and α2-antiplasmin can also affect the function of this complex, potentially leading to disorders of the blood clotting system.

See also

• Fibrinolysis
• Plasmin
• α2-antiplasmin

References

Plasmin-α2-antiplasmin Resources
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