help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published May 18, 2007. doi:10.1529/biophysj.107.105171
© 2007 by the Biophysical Society.

A more recent version of this article appeared on August 1, 2007.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.107.105171v1
93/3/859    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Cadugan, D. J.
Right arrow Articles by Auerbach, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cadugan, D. J.
Right arrow Articles by Auerbach, A.

CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

Conformational dynamics of the {alpha}M3 transmembrane helix during acetylcholine receptor-channel gating

David J. Cadugan 1 and Anthony Auerbach 1*

1 SUNY at Buffalo

* To whom correspondence should be addressed. E-mail: auerbach{at}buffalo.edu.

Submitted on January 24, 2007
Revised on March 9, 2007
Accepted on 12 April 2007


  Abstract
Muscle acetylcholine receptors (AChRs) are synaptic ion channels that 'gate' between closed- and open-channel conformations. We used {Phi}-value analysis (1, 2) to probe the relative timing of the gating motions of the residues in the M3, membrane-spanning helix of the AChR {alpha}-subunit. In the upper half of {alpha}M3 the gating motions of all five tested residues are temporally correlated ({Phi}{approx}0.30) and serve to link structural changes occurring at the middle of the M2, pore-lining helix with those occurring at the interface of the extracellular and transmembrane domains. {alpha}M3 belongs to a complex and diverse set of synchronously-moving parts that change structure relatively late in the channel-opening process. The propagation of the gating Brownian conformational cascade has a complex spatial distribution in the transmembrane domain.

Key Words: REFER, cys-loop, ion channel, single-channel, transition state




This article has been cited by other articles:


Home page
 JGPHome page
P. Purohit and A. Auerbach
Acetylcholine Receptor Gating at Extracellular Transmembrane Domain Interface: the "Pre-M1" Linker
J. Gen. Physiol., November 26, 2007; 130(6): 559 - 568.
[Abstract] [Full Text] [PDF]

Home page
 JGPHome page
A. Jha, D. J. Cadugan, P. Purohit, and A. Auerbach
Acetylcholine Receptor Gating at Extracellular Transmembrane Domain Interface: the Cys-Loop and M2 M3 Linker
J. Gen. Physiol., November 26, 2007; 130(6): 547 - 558.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2007 by the Biophysical Society.