The Journal of General Physiology
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Published 1 January 2000. doi:10.1085/jgp.115.1.51
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© The Rockefeller University Press, 0022-1295/2000//51/ $5.00
Journal of General Physiology, Volume 115, Number 1, 2000

Original Article

The Lipid–Protein Interface of aShaker K+ Channel

Kwang Hee Honga and Christopher Millera

a From the Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02454-9110
Department of Biochemistry, Brandeis University, 415 South Street, HHMI, Waltham, MA 02454-9110.781-736-2365

cmiller{at}brandeis.edu

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 Kv channels.

Key Words: tryptophan-scanning • {alpha}-helix • gating

© 2000 The Rockefeller University Press


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