期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：2003
卷号：100
期号：22
页码：12607-12612
DOI：10.1073/pnas.2235650100
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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 Kv{beta}2-subunit. By using a difference map between the full-length and truncated Shaker -{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 Kv{beta}2-subunit, suggests a possible mechanism for the modulation of the K+ voltage-gated channel function by its {beta}-subunit.
关键词：C-terminal deletion ; electron microscopy ; single-particle analysis
