Conformational changes in the C terminus of Shaker K+ channel bound to the rat Kvβ2-subunit Academic Article uri icon


MeSH Major

  • Potassium Channels
  • Potassium Channels, Voltage-Gated
  • Protein Conformation


  • 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.

publication date

  • October 28, 2003



  • Academic Article



  • eng

PubMed Central ID

  • PMC240665

Digital Object Identifier (DOI)

  • 10.1073/pnas.2235650100

PubMed ID

  • 14569011

Additional Document Info

start page

  • 12607

end page

  • 12


  • 100


  • 22