Structure−Activity Relationships for the Interaction of Bovine Pancreatic Trypsin Inhibitor with an Intracellular Site on a Large Conductance Ca2+-Activated K+ Channel

Large conductance Ca2+-activated K+ channels (BKCa) contain an intracellular binding site for bovine pancreatic trypsin inhibitor (BPTI), a well-known inhibitor of various serine proteinase (SerP) enzymes. To investigate the structural basis of this interaction, we examined the activity of 11 BPTI m...

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Bibliographic Details
Published in:Biochemistry (Easton) 2000-02, Vol.39 (8), p.2001-2012
Main Authors: Favre, Isabelle, Moss, Guy W. J, Goldenberg, David P, Otlewski, Jacek, Moczydlowski, Edward
Format: Article
Language:English
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Summary:Large conductance Ca2+-activated K+ channels (BKCa) contain an intracellular binding site for bovine pancreatic trypsin inhibitor (BPTI), a well-known inhibitor of various serine proteinase (SerP) enzymes. To investigate the structural basis of this interaction, we examined the activity of 11 BPTI mutants using single BKCa channels from rat skeletal muscle incorporated into planar lipid bilayers. All of the mutants induced discrete substate events at the single-channel level. The dwell time of the substate, which is inversely related to the dissociation rate constant of BPTI, exhibited relatively small changes (
ISSN:0006-2960
1520-4995
DOI:10.1021/bi992140v