2l0j
From Proteopedia
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- | [[ | + | ==Solid State NMR structure of the M2 proton channel from Influenza A Virus in hydrated lipid bilayer== |
+ | <StructureSection load='2l0j' size='340' side='right' caption='[[2l0j]], [[NMR_Ensembles_of_Models | 8 NMR models]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2l0j]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus Influenza a virus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L0J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L0J FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 Influenza A virus])</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l0j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l0j RCSB], [http://www.ebi.ac.uk/pdbsum/2l0j PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The M2 protein from the influenza A virus, an acid-activated proton-selective channel, has been the subject of numerous conductance, structural, and computational studies. However, little is known at the atomic level about the heart of the functional mechanism for this tetrameric protein, a His(37)-Trp(41) cluster. We report the structure of the M2 conductance domain (residues 22 to 62) in a lipid bilayer, which displays the defining features of the native protein that have not been attainable from structures solubilized by detergents. We propose that the tetrameric His(37)-Trp(41) cluster guides protons through the channel by forming and breaking hydrogen bonds between adjacent pairs of histidines and through specific interactions of the histidines with the tryptophan gate. This mechanism explains the main observations on M2 proton conductance. | ||
- | + | Insight into the mechanism of the influenza A proton channel from a structure in a lipid bilayer.,Sharma M, Yi M, Dong H, Qin H, Peterson E, Busath DD, Zhou HX, Cross TA Science. 2010 Oct 22;330(6003):509-12. PMID:20966252<ref>PMID:20966252</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels|Ion channels]] | ||
*[[M2 protein|M2 protein]] | *[[M2 protein|M2 protein]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Influenza a virus]] | [[Category: Influenza a virus]] | ||
[[Category: Busath, D D.]] | [[Category: Busath, D D.]] |
Revision as of 04:20, 29 September 2014
Solid State NMR structure of the M2 proton channel from Influenza A Virus in hydrated lipid bilayer
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