Bovine pancreatic trypsin inhibitor as a probe of large conductance Ca(2+)-activated K+ channels at an internal site of interaction

Bovine pancreatic trypsin inhibitor (BPTI) is a 58 residue protein whose binding to various serine proteases has been extensively studied by X-ray crystallography. We have found that BPTI also binds to an intracellular site associated with the large conductance Ca(2+)-activated K+ channel, as detect...

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Veröffentlicht in:	Biochemical pharmacology 1992-01, Vol.43 (1), p.21-28
Hauptverfasser:	Moczydlowski, E, Moss, G W, Lucchesi, K J
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Aprotinin - chemistry Aprotinin - pharmacology Binding Sites - drug effects Calcium - metabolism Cattle Elapid Venoms - chemistry Elapid Venoms - pharmacology Electric Conductivity Models, Chemical Molecular Sequence Data Potassium Channels - drug effects
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creator	Moczydlowski, E Moss, G W Lucchesi, K J
description	Bovine pancreatic trypsin inhibitor (BPTI) is a 58 residue protein whose binding to various serine proteases has been extensively studied by X-ray crystallography. We have found that BPTI also binds to an intracellular site associated with the large conductance Ca(2+)-activated K+ channel, as detected by the production of subconductance events in single channels incorporated into planar lipid bilayers. BPTI is highly homologous to a family of mamba snake dendrotoxin proteins that inhibit various K+ channels at an extracellular site. BPTI thus provides a useful model system to explore basic mechanisms underlying protein-channel interactions.
doi_str_mv	10.1016/0006-2952(92)90656-4
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source	MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects	Amino Acid Sequence Animals Aprotinin - chemistry Aprotinin - pharmacology Binding Sites - drug effects Calcium - metabolism Cattle Elapid Venoms - chemistry Elapid Venoms - pharmacology Electric Conductivity Models, Chemical Molecular Sequence Data Potassium Channels - drug effects
title	Bovine pancreatic trypsin inhibitor as a probe of large conductance Ca(2+)-activated K+ channels at an internal site of interaction
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