The lipid-protein interface of a Shaker K(+) channel.
Tryptophan-substitution mutagenesis was applied to the first and third transmembrane segments (S1 and S3) of a Shaker-type K(+) channel for the purpose of ascertaining whether these sequences are alpha-helical. Point mutants were examined for significant functional changes, indicated by the voltage-activation curves and gating kinetics. Helical periodicity of functional alteration was observed throughout the entire S1 segment. A similar result was obtained with the first 14 residues of S3, but this periodicity disappeared towards the extracellular side of this transmembrane sequence. In both helical stretches, tryptophan-tolerant positions are clustered on approximately half the alpha-helix surface, as if the sidechains are exposed to the hydrocarbon region of the lipid bilayer. These results, combined with an analogous study of S2 (Monks, S., D.J. Needleman, and C. Miller. 1999. J. Gen. Physiol. 113:415-423), locate S1, S2, and S3 on the lipid-facing periphery of K(v) channels.
Hong
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Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454-9110, USA.
Miller
C
C
D000818:Animals; D015640:Ion Channel Gating / Q000502:physiology*; D008051:Lipid Bilayers / Q000737:chemistry*; D016296:Mutagenesis; D010507:Periodicity; D017354:Point Mutation; D015221:Potassium Channels / Q000737:chemistry* / Q000502:physiology; D017433:Protein Structure, Secondary / Q000502:physiology*; D051637:Shaker Superfamily of Potassium Channels; D014981:Xenopus
D008051:Lipid Bilayers; D015221:Potassium Channels; D051637:Shaker Superfamily of Potassium Channels