Abstract
We report our progress in understanding the structure-function relationships for the interaction between BPTI and serine proteases. We focused on extensive mutagenesis of four crucial positions from the protease binding loop of BPTI. Selected variants were characterized by determination of association constants, stability parameters and structures of protease-inhibitor complexes.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Aprotinin / metabolism*
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Chymotrypsin / chemistry
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Enzyme Stability
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Protein Binding
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Serine Endopeptidases / metabolism*
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Serine Proteinase Inhibitors / metabolism*
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Structure-Activity Relationship
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Trypsin / chemistry
Substances
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Serine Proteinase Inhibitors
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Aprotinin
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Serine Endopeptidases
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Chymotrypsin
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Trypsin