[HTML][HTML] The serpins are an expanding superfamily of structurally similar but functionally diverse proteins
GA Silverman, PI Bird, RW Carrell, FC Church… - Journal of Biological …, 2001 - ASBMB
The serpins (serine proteinase inhibitors) are a superfamily of proteins (350–500 amino
acids in size) that fold into a conserved structure and employ a unique suicide substrate-like
inhibitory mechanism. The serpins were last reviewed in 1994 (1). More recent studies
show: 1) an expanded distribution within the kingdoms of metazoa and plantae, as well as
certain viruses, 2) a surprising effect on the covalently bound target proteinase, and 3) novel
biochemical and biological functions. Most serpins inhibit serine proteinases of the …
acids in size) that fold into a conserved structure and employ a unique suicide substrate-like
inhibitory mechanism. The serpins were last reviewed in 1994 (1). More recent studies
show: 1) an expanded distribution within the kingdoms of metazoa and plantae, as well as
certain viruses, 2) a surprising effect on the covalently bound target proteinase, and 3) novel
biochemical and biological functions. Most serpins inhibit serine proteinases of the …