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The alpha-helix and the organization and gating of channels

Spencer, Robert H. and Rees, ­Douglas C. (2002) The alpha-helix and the organization and gating of channels. Annual Review of Biophysics and Biomolecular Structure, 31 . pp. 207-233. ISSN 1056-8700. http://resolver.caltech.edu/CaltechAUTHORS:SPEarbbs02

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Abstract

The structures of an increasing number of channels and other a-helical membrane proteins have been determined recently, including the KcsA potassium channel, the MscL mechanosensitive channel, and the AQP1 and GlpF members of the aquaporin family. In this chapter, the orientation and packing characteristics of bilayer-spanning helices are surveyed in integral membrane proteins. In the case of channels, a-helices create the scaled barrier that separates the hydrocarbon region of the bilayer from the permeation pathway for solutes. The helices surrounding the permeation pathway tend to be rather steeply tilted relative to the membrane normal and are consistently arranged in a right-handed bundle. The helical framework further provides a supporting scaffold for nonmembrane-spanning structures associated with channel selectivity. Although structural details remain scarce, the conformational changes associated with gating transitions between closed and open states of channels are reviewed, emphasizing the potential roles of helix-helix interactions in this process.


Item Type:Article
Additional Information:"Reprinted, with permission, from the Annual Review of Biophysics and Biomolecular Structure, Volume 31 copyright 2002 by Annual Reviews, www.annualreviews.org" Discussions with Randal Bass, Kaspar Locher, Pavel Strop, Allen Lee, Margaret Barclay, Dennis Dougherty, Henry Lester, and Chris Miller are greatly appreciated. This work was supported in part by NIH grant GM62532.
Subject Keywords:ION CHANNELS; MEMBRANE PROTEINS; TRANSMEMBRANE HELICES; CONFORMATIONAL CHANGES; MECHANOSENSITIVE ION-CHANNEL; PHOTOSYNTHETIC REACTION-CENTER; CYTOCHROME-C-OXIDASE; GATED K+ CHANNEL; SHAKER POTASSIUM CHANNEL; PROTEIN-DATA-BANK; MEMBRANE-PROTEINS; ESCHERICHIA-COLI; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE
Record Number:CaltechAUTHORS:SPEarbbs02
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:SPEarbbs02
Alternative URL:http://dx.doi.org/10.1146/annurev.biophys.31.082901.134329
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:1567
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:30 Jan 2006
Last Modified:26 Dec 2012 08:45

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