Department of Anesthesiology

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Conformational changes in the C terminus of Shaker K+ channel bound to the rat Kvbeta2-subunit.

TitleConformational changes in the C terminus of Shaker K+ channel bound to the rat Kvbeta2-subunit.
Publication TypeJournal Article
Year of Publication2003
AuthorsSokolova O, Accardi A, Gutierrez D, Lau A, Rigney M, Grigorieff N
JournalProc Natl Acad Sci U S A
Volume100
Issue22
Pagination12607-12
Date Published2003 Oct 28
ISSN0027-8424
KeywordsAnimals, Binding Sites, Cercopithecus aethiops, COS Cells, Fourier Analysis, Models, Molecular, Peptide Fragments, Potassium Channels, Potassium Channels, Voltage-Gated, Protein Conformation, Protein Subunits, Rats, Recombinant Proteins, Restriction Mapping, Shaker Superfamily of Potassium Channels, Transfection
Abstract

We studied the structure of the C terminus of the Shaker potassium channel. The 3D structures of the full-length and a C-terminal deletion (Delta C) mutant of Shaker were determined by electron microscopy and single-particle analysis. The difference map between the full-length and the truncated channels clearly shows a compact density, located on the sides of the T1 domain, that corresponds to a large part of the C terminus. We also expressed and purified both WT and Delta C Shaker, assembled with the rat KvBeta2-subunit. By using a difference map between the full-length and truncated Shaker alpha-beta complexes, a conformational change was identified that shifts a large part of the C terminus away from the membrane domain and into close contact with the Beta-subunit. This conformational change, induced by the binding of the KvBeta2-subunit, suggests a possible mechanism for the modulation of the K+ voltage-gated channel function by its Beta-subunit.

DOI10.1073/pnas.2235650100
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID14569011
PubMed Central IDPMC240665
Grant ListP01 GM 62580 / GM / NIGMS NIH HHS / United States
R01 GM 63012-01A1 / GM / NIGMS NIH HHS / United States