The structural puzzle of how serpin serine proteinase inhibitors work

Serine proteinase cleavage of proteins is essential to a wide variety of biological processes and is primarily regulated by protein inhibitors. Many inhibitors are conformationally rigid simulations of optimal serine proteinase substrates, which makes them highly efficient competitive inhibitors of...

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Bibliographic Details
Published inBioEssays Vol. 18; no. 6; p. 453
Main Author Wright, H T
Format Journal Article
LanguageEnglish
Published United States 01.06.1996
Subjects
Amino Acid Sequence
Animals
Binding Sites - genetics
Humans
Models, Molecular
Molecular Sequence Data
Molecular Structure
Polymorphism, Genetic
Protein Conformation
Protein Structure, Secondary
Serpins - chemistry
Serpins - genetics
Serpins - metabolism
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Summary:Serine proteinase cleavage of proteins is essential to a wide variety of biological processes and is primarily regulated by protein inhibitors. Many inhibitors are conformationally rigid simulations of optimal serine proteinase substrates, which makes them highly efficient competitive inhibitors of target proteinases. In contrast, members of the serpin family of serine proteinase inhibitors display extensive flexibility and polymorphism, particularly in their reactive site segments and in beta-sheet secondary structure, which can take up and expel strands. Reactive site and beta-sheet polymorphism appear to be coupled in the serpins and may account for the extreme stability of serpin-proteinase complexes through the insertion of the reactive site strand into a beta-sheet. These unusual properties may have opened an adaptive pathway of proteinase regulation that was unavailable to the conformationally rigid proteinase inhibitors.
ISSN:0265-9247
1521-1878
DOI:10.1002/bies.950180607