Structure-function relationships in serine protease-bovine pancreatic trypsin inhibitor interaction.
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.
Krowarsch
D
D
Institute of Biochemistry & Molecular Biology, University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland.
Zakrzewska
M
M
Smalas
A O
AO
Otlewski
J
J
D007611:Aprotinin / Q000378:metabolism*; D002918:Chymotrypsin / Q000737:chemistry; D004795:Enzyme Stability; D011485:Protein Binding; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000737:chemistry
D015842:Serine Proteinase Inhibitors; D007611:Aprotinin; D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin