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PMID: 7506933 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Intimations of K+ channel structure from a complete functional map of the molecular surface of charybdotoxin.

Biochemistry ·Vol. 33 ·No. 2 ·1994-01-18 ·Pages 443-50

Stampe P, Kolmakova-Partensky L, Miller C

Abstract

The external vestibules of many K+ channels carry a high-affinity receptor for charybdotoxin, a peptide of known structure. Point mutations of a recombinant toxin identified the residues directly involved in the interaction with a Ca(2+)-activated K+ channel. The interaction surface is formed from 8 of the 37 residues and covers about 25% of the peptide's molecular surface. The shape of the toxin permits a deduced picture of the complementary receptor site in the external vestibule of the K+ channel.

MeSH Terms
Amino Acid Sequence Animals Binding Sites Calcium/pharmacology Charybdotoxin Chemical Phenomena Chemistry, Physical Kinetics Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data Molecular Structure Point Mutation Potassium Channels/chemistry,metabolism Protein Folding Protein Structure, Secondary Rats Recombinant Proteins/chemistry Scorpion Venoms/chemistry,genetics,metabolism
Chemicals
Potassium Channels Recombinant Proteins Scorpion Venoms Charybdotoxin Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stampe P
Howard Hughes Medical Institute, Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254-9110.
Kolmakova-Partensky L
Miller C
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1994-01-18
Pages
443-50
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIGMS NIH HHS · GM-31768 · United States
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