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- W2009304073 abstract "The mechanism of formation and the structures of serpin–inhibitor complexes are not completely understood, despite detailed knowledge of the structures of a number of cleaved and uncleaved inhibitor, noninhibitor, and latent serpins. It has been proposed from comparison of inhibitor and noninhibitor serpins in the cleaved and uncleaved forms that insertion of strand s4A into preexisting β-sheet A is a requirement for serpin inhibitor activity. We have investigated the role of this strand in formation of serpin–proteinase complexes and in serpin inhibitor activity through homology modeling of wild type inhibitor, mutant substrate, and latent serpins, and of putative serpin–proteinase complexes. These models explain the high stability of the complexes and provide an understanding of substrate behavior in serpins with point mutations in s4A and of latency in plasmingoen activator inhibitor I. © 1995 Wiley-Liss, Inc." @default.
- W2009304073 created "2016-06-24" @default.
- W2009304073 creator A5021077783 @default.
- W2009304073 creator A5025444311 @default.
- W2009304073 date "1995-07-01" @default.
- W2009304073 modified "2023-10-06" @default.
- W2009304073 title "Structural basis for serpin inhibitor activity" @default.
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- W2009304073 doi "https://doi.org/10.1002/prot.340220303" @default.
- W2009304073 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7479695" @default.