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PMID: 8038378 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Mutations in the K+ channel signature sequence.

Biophysical journal ·Vol. 66 ·No. 4 ·1994-04-00 ·Pages 1061-7

Heginbotham L, Lu Z, Abramson T, MacKinnon R

Abstract

Potassium channels share a highly conserved stretch of eight amino acids, a K+ channel signature sequence. The conserved sequence falls within the previously defined P-region of voltage-activated K+ channels. In this study we investigate the effect of mutations in the signature sequence of the Shaker channel on K+ selectivity determined under bi-ionic conditions. Nonconservative substitutions of two threonine residues and the tyrosine residue leave selectivity intact. In contrast, mutations at some positions render the channel nonselective among monovalent cations. These findings are consistent with a proposal that the signature sequence contributes to a selectivity filter. Furthermore, the results illustrate that the hydroxyl groups at the third and fourth positions, and the aromatic group at position seven, are not essential in determining K+ selectivity.

MeSH Terms
Amino Acid Sequence Animals Biophysical Phenomena Biophysics Conserved Sequence Drosophila/genetics Female In Vitro Techniques Molecular Sequence Data Mutagenesis, Site-Directed Mutation Oocytes/metabolism Phenotype Potassium/metabolism Potassium Channels/genetics,metabolism Sequence Homology, Amino Acid Xenopus laevis
Chemicals
Potassium Channels Potassium
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Heginbotham L
Department of Neurology, Harvard Medical School, Boston, Massachusetts 02115.
Lu Z
Abramson T
MacKinnon R
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
Published
1994-04-00
Pages
1061-7
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1275813
Subset
IM
Grants
NIGMS NIH HHS · GM47400 · United States
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