2h95
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(New page: 200px<br /><applet load="2h95" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h95" /> '''Structure of the Amantadine-Blocked Influenz...)
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Revision as of 12:42, 23 January 2008
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Structure of the Amantadine-Blocked Influenza A M2 Proton Channel Trans-membrane Domain by Solid-state NMR spectroscopy
Overview
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 degrees and 28 degrees 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.
About this Structure
2H95 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Backbone Structure of the Amantadine-blocked Trans-membrane Domain M2 Proton Channel from Influenza A Virus., Hu J, Asbury TM, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA, Biophys J. 2007 Mar 23;. PMID:17384070
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