Serpin
Serpin
Serpin (pronounced: /ˈsɜːrpɪn/), is a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. The name 'serpin' is an acronym for Serine Protease INhibitors.
Etymology
The term "serpin" is derived from their function as serine protease inhibitors. Serine proteases are enzymes that cut other proteins at specific sites and serpins control these enzymes by forming a covalent bond with them, which stops their activity.
Function
Serpins are a group of proteins with diverse functions, including control of blood clotting, inflammation, immune response and cell death. They achieve these diverse roles by using a conformational change to inhibit target proteins. This makes them a unique class of protease inhibitors.
Related Terms
- Protease: An enzyme that conducts proteolysis, protein catabolism by hydrolysis of peptide bonds.
- Enzyme: Macromolecular biological catalysts that accelerate chemical reactions.
- Proteolysis: The breakdown of proteins into smaller polypeptides or amino acids.
- Covalent bond: A chemical bond that involves the sharing of electron pairs between atoms.
- Inflammation: A part of the complex biological response of body tissues to harmful stimuli, such as pathogens, damaged cells, or irritants.
- Immune response: The reaction of the cells and fluids of the body to the presence of a substance which is not recognized as a constituent of the body itself.
See Also
External links
- Medical encyclopedia article on Serpin
- Wikipedia's article - Serpin
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