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Wikipedia:Today's featured article/requests/Serpin

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Serpin

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This is the archived discussion of the TFAR nomination for the article below. Subsequent comments should be made on the appropriate discussion page (such as Wikipedia talk:Today's featured article/requests). Please do not modify this page.

The result was: scheduled for Wikipedia:Today's featured article/April 2, 2016 by  — Chris Woodrich (talk) 00:37, 18 March 2016 (UTC)[reply]

A serpin (white) with its 'reactive centre loop' (blue) bound to a protease (grey). Once the protease attempts catalysis it will be irreversibly inhibited. (PDB: 1K9O​)

Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. They 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. Protease inhibition by serpins controls an array of biological processes, including coagulation and inflammation, and consequently these proteins are the target of medical research. Their conformational-change mechanism confers certain advantages, but it also has drawbacks: serpins are vulnerable to mutations that can result in serpinopathies such as protein misfolding and the formation of inactive long-chain polymers. Serpin polymerisation not only reduces the amount of active inhibitor, but also leads to accumulation of the polymers, causing cell death and organ failure. (Full article...)