The lipid-protein interface of a Shaker K+ channel

被引:107
作者
Hong, KH [1 ]
Miller, C [1 ]
机构
[1] Brandeis Univ, Howard Hughes Med Inst, Dept Biochem, Waltham, MA 02454 USA
关键词
tryptophan-scanning; alpha-helix; gating;
D O I
10.1085/jgp.115.1.51
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
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 to towards the extracellular side of this transmembrane sequence. In both helical stretches, tryptophan-tolerant positions are clustered on approximately half die 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.
引用
收藏
页码:51 / 58
页数:8
相关论文
共 15 条
[1]   Gapped BLAST and PSI-BLAST: a new generation of protein database search programs [J].
Altschul, SF ;
Madden, TL ;
Schaffer, AA ;
Zhang, JH ;
Zhang, Z ;
Miller, W ;
Lipman, DJ .
NUCLEIC ACIDS RESEARCH, 1997, 25 (17) :3389-3402
[2]   An alpha-carbon template for the transmembrane helices in the rhodopsin family of G-protein-coupled receptors [J].
Baldwin, JM ;
Schertler, GFX ;
Unger, VM .
JOURNAL OF MOLECULAR BIOLOGY, 1997, 272 (01) :144-164
[3]   Three distinct structural environments of a transmembrane domain in the inwardly rectifying potassium channel ROMK1 defined by perturbation [J].
Choe, S ;
Stevens, CF ;
Sullivan, JM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (26) :12046-12049
[4]  
DONNELLY D, 1993, PROTEIN SCI, V2, P55
[5]   The structure of the potassium channel:: Molecular basis of K+ conduction and selectivity [J].
Doyle, DA ;
Cabral, JM ;
Pfuetzner, RA ;
Kuo, AL ;
Gulbis, JM ;
Cohen, SL ;
Chait, BT ;
MacKinnon, R .
SCIENCE, 1998, 280 (5360) :69-77
[6]   BIOPHYSICAL AND MOLECULAR MECHANISMS OF SHAKER POTASSIUM CHANNEL INACTIVATION [J].
HOSHI, T ;
ZAGOTTA, WN ;
ALDRICH, RW .
SCIENCE, 1990, 250 (4980) :533-538
[7]   SUBUNIT STOICHIOMETRY OF A MAMMALIAN K+ CHANNEL DETERMINED BY CONSTRUCTION OF MULTIMERIC CDNAS [J].
LIMAN, ER ;
TYTGAT, J ;
HESS, P .
NEURON, 1992, 9 (05) :861-871
[8]   Chemical basis for alkali cation selectivity in potassium-channel proteins [J].
Moczydlowski, E .
CHEMISTRY & BIOLOGY, 1998, 5 (11) :R291-R301
[9]   Helical structure and packing orientation of the S2 segment in the Shaker K+ channel [J].
Monks, SA ;
Needleman, DJ ;
Miller, C .
JOURNAL OF GENERAL PHYSIOLOGY, 1999, 113 (03) :415-423
[10]   ELECTROSTATIC INTERACTIONS OF S4 VOLTAGE SENSOR IN SHAKER K+ CHANNEL [J].
PAPAZIAN, DM ;
SHAO, XM ;
SEOH, SA ;
MOCK, AF ;
HUANG, Y ;
WAINSTOCK, DH .
NEURON, 1995, 14 (06) :1293-1301