We are seeing patients in-person and through Video Visits. Learn more about how we’re keeping you safe and please review our updated visitor policy. Please also consider supporting Weill Cornell Medicine’s efforts to support our front-line workers.
Department of Anesthesiology

You are here

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