Serpins are a superfamily of proteins, whose membership is based on the presence of a
single common core domain consisting of three β-sheets and 8-9 R-helices, and with a set of …

Serpins are a broadly distributed family of protease inhibitors that use a conformational
change to inhibit target enzymes. They are central in controlling many important proteolytic …

Limited proteolysis is responsible for activating a wide range of proteins from immature
forms and is hence implicated in a number of biologically imporw x tant systems 1–3 …

Proteinase inhibitors of the serpin family have a unique ability to regulate their activity by
changing the conformation of their reactive-centre loop. Although this may explain their …

Point mutations cause members of the serine protease inhibitor (serpin) superfamily to
undergo a novel conformational transition, forming ordered polymers. These polymers …

Food gels have many useful properties. Globular protein gels are more nutritious than
polysaccharide gels, but most are not as transparent as agarose or gelatin gels. However …

We reported previously that human interleukin-1 beta converting enzyme (ICE) is regulated
by the CrmA serpin encoded by cowpox virus. We now report the mechanism and kinetics of …

Background Antithrombin, a member of the serpin family of inhibitors, controls coagulation in
human plasma by forming complexes with thrombin and other coagulation proteases in a …

Serine proteinase inhibitors (Serpins) are irreversible suicide inhibitors of proteases that
regulate diverse physiological processes such as coagulation, fibrinolysis, complement …

The reactive site loop of the serpin family of serine proteinase inhibitors is flexible and can
adopt a number of diverse conformations. A 2.9 Å resolution structure of α1-antitrypsin—the …