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.
Keywords: protein-protein recognition, serine protease, canonical protein inhibitor, protein stability
Protein & Peptide Letters
Title: Structure-Function Relationships in Serine Protease-Bovine Pancreatic Trypsin Inhibitor Interaction
Volume: 12 Issue: 5
Author(s): D. Krowarsch, M. Zakrzewska, A. O. Smalas and J. Otlewski
Affiliation:
Keywords: protein-protein recognition, serine protease, canonical protein inhibitor, protein stability
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.
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Cite this article as:
Krowarsch D., Zakrzewska M., Smalas O. A. and Otlewski J., Structure-Function Relationships in Serine Protease-Bovine Pancreatic Trypsin Inhibitor Interaction, Protein & Peptide Letters 2005; 12 (5) . https://dx.doi.org/10.2174/0929866054395275
DOI https://dx.doi.org/10.2174/0929866054395275 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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