help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Biophys. J. BioFAST: First Published March 23, 2007. doi:10.1529/biophysj.106.090183
© 2007 by the Biophysical Society.

A more recent version of this article appeared on June 15, 2007.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.106.090183v1
92/12/4335    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 Hu, J.
Right arrow Articles by Cross, T. A
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hu, J.
Right arrow Articles by Cross, T. A

CHANNELS, RECEPTORS, AND ELECTRICAL SIGNALING

Backbone Structure of the Amantadine-blocked Trans-membrane Domain M2 Proton Channel from Influenza A Virus

Jun Hu 1, Tom M. Asbury 2*, Srisairam Achuthan 2, Congang Li 2, Richard Bertram 2, Jack R Quine 3, Riqiang Fu 2 and Tim A Cross 2

1 NIDDK, National Institutes of Health
2 Florida State University
3 Florda State University

* To whom correspondence should be addressed. E-mail: tasbu{at}sb.fsu.edu.

Submitted on May 26, 2006
Revised on July 14, 2006
Accepted on 1 February 2007


  Abstract
Amantadine is known to block the M2 proton channel of the Influenza A virus. Here, we present a structure of the M2trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid state NMR PISEMA experiments.The data indicates a kink in the monomer between two helical fragments having 19° and 28° tilt angles with respect to the membrane normal. This monomer structure is then used to construct a plausible model of the tetrameric amantadine-blocked M2 trans-membrane channel. The influence of amantadine binding through comparative Cross Polarization Magic Angle Spinning (CPMAS) spectra was alsoobserved. In addition, spectra are shown of the amantadine resistant mutant, S31N, in the presence and absence of amantadine.

Key Words: Influenxa A, M2 Protein, PISEMA, amantadine, membrane proteins, solid-state NMR




This article has been cited by other articles:


Home page
 Biophys. JHome page
C. Li, M. Yi, J. Hu, H.-X. Zhou, and T. A. Cross
Solid-State NMR and MD Simulations of the Antiviral Drug Amantadine Solubilized in DMPC Bilayers
Biophys. J., February 15, 2008; 94(4): 1295 - 1302.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. D. Cady and M. Hong
Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
PNAS, February 5, 2008; 105(5): 1483 - 1488.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
H. Chen, Y. Wu, and G. A. Voth
Proton Transport Behavior through the Influenza A M2 Channel: Insights from Molecular Simulation
Biophys. J., November 15, 2007; 93(10): 3470 - 3479.
[Abstract] [Full Text] [PDF]


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