2h95
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Amantadine is known to block the M2 proton channel of the Influenza A | + | Amantadine is known to block the M2 proton channel of the Influenza A virus. Here, we present a structure of the M2 trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid-state NMR polarization-inversion-spin-exchange-at-the-magic-angle experiments. The data indicates a kink in the monomer between two helical fragments having 20 degrees and 31 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 spectra was also observed. In addition, spectra are shown of the amantadine-resistant mutant, S31N, in the presence and absence of amantadine. |
==About this Structure== | ==About this Structure== | ||
| Line 10: | Line 10: | ||
==Reference== | ==Reference== | ||
| - | Backbone | + | Backbone structure of the amantadine-blocked trans-membrane domain M2 proton channel from Influenza A virus., Hu J, Asbury T, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA, Biophys J. 2007 Jun 15;92(12):4335-43. Epub 2007 Mar 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17384070 17384070] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Asbury, T.]] | [[Category: Asbury, T.]] | ||
| - | [[Category: Cross, T | + | [[Category: Cross, T A.]] |
[[Category: Hu, J.]] | [[Category: Hu, J.]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
[[Category: protein-ligand]] | [[Category: protein-ligand]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:39:28 2008'' |
Revision as of 15:39, 21 February 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 M2 trans-membrane domain blocked with amantadine, built using orientational constraints obtained from solid-state NMR polarization-inversion-spin-exchange-at-the-magic-angle experiments. The data indicates a kink in the monomer between two helical fragments having 20 degrees and 31 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 spectra was also observed. 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 T, Achuthan S, Li C, Bertram R, Quine JR, Fu R, Cross TA, Biophys J. 2007 Jun 15;92(12):4335-43. Epub 2007 Mar 23. PMID:17384070
Page seeded by OCA on Thu Feb 21 17:39:28 2008
