How Serpins Are Shaping Up

See allHide authors and affiliations

Science  17 Sep 1999:
Vol. 285, Issue 5435, pp. 1861-1863
DOI: 10.1126/science.285.5435.1861

You are currently viewing the summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


The serpins are a versatile family of serine protease inhibitors that are involved in coagulation, fibrinolysis, and many other physiological processes. In a Perspective, Carrell discusses new findings that reveal that small conformational changes in a serpin after cleavage of its reactive site by a target protease can result in acquisition of new functions. For example, O'Reilly et al. demonstrate that small conformational changes in antithrombin III result in a switch from its job as an inhibitor of clotting enzymes to a new function as an inhibitor of blood vessel formation and tumor progression.