Serpin (nonfiction)

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A serpin (white) with its 'reactive centre loop' (blue) bound to a protease (grey). Once the protease attempts catalysis it will be irreversibly inhibited.

Serpins are a superfamily of proteins, notable for their irreversible protease inhibition of target proteases.

Serins are notable for their unusual mechanism of action, in which they irreversibly inhibit their target protease by undergoing a large conformational change to disrupt its active site.

This contrasts with the more common competitive mechanism for protease inhibitors that bind to and block access to the protease active site.

Serpins are found in all kingdoms of life.

The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (serine protease inhibitors).

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