2h95: Difference between revisions
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==Structure of the Amantadine-Blocked Influenza A M2 Proton Channel Trans-membrane Domain by Solid-state NMR spectroscopy== | |||
<StructureSection load='2h95' size='340' side='right'caption='[[2h95]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2h95]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/USSR/90/1977(H1N1)) Influenza A virus (A/USSR/90/1977(H1N1))]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H95 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H95 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h95 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h95 OCA], [https://pdbe.org/2h95 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h95 RCSB], [https://www.ebi.ac.uk/pdbsum/2h95 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h95 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
'' | [https://www.uniprot.org/uniprot/Q3LZC0_9INFA Q3LZC0_9INFA] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
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. | 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. | ||
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<ref>PMID:17384070</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2h95" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
*[[M2 protein|M2 protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Asbury T]] | |||
[[Category: Cross TA]] | |||
[[Category: Hu J]] | |||
Latest revision as of 16:37, 13 December 2023
Structure of the Amantadine-Blocked Influenza A M2 Proton Channel Trans-membrane Domain by Solid-state NMR spectroscopy
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