2lwa
From Proteopedia
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| - | + | ==Conformational ensemble for the G8A mutant of the influenza hemagglutinin fusion peptide== | |
| - | + | <StructureSection load='2lwa' size='340' side='right' caption='[[2lwa]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lwa]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/hong_kong/1035/1998(h1n1)) Influenza a virus (a/hong kong/1035/1998(h1n1))]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LWA FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kxa|2kxa]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lwa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lwa RCSB], [http://www.ebi.ac.uk/pdbsum/2lwa PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The highly conserved first 23 residues of the influenza hemagglutinin HA2 subunit constitute the fusion domain, which plays a pivotal role in fusing viral and host-cell membranes. At neutral pH, this peptide adopts a tight helical hairpin wedge structure, stabilized by aliphatic hydrogen bonding and charge-dipole interactions. We demonstrate that at low pH, where the fusion process is triggered, the native peptide transiently visits activated states that are very similar to those sampled by a G8A mutant. This mutant retains a small fraction of helical hairpin conformation, in rapid equilibrium with at least two open structures. The exchange rate between the closed and open conformations of the wild-type fusion peptide is approximately 40 kHz, with a total open-state population of approximately 20%. Transitions to these activated states are likely to play a crucial role in formation of the fusion pore, an essential structure required in the final stage of membrane fusion. | ||
| - | + | pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.,Lorieau JL, Louis JM, Schwieters CD, Bax A Proc Natl Acad Sci U S A. 2012 Nov 19. PMID:23169643<ref>PMID:23169643</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Bax, A | + | == References == |
| - | [[Category: Lorieau, J L | + | <references/> |
| - | [[Category: Louis, J M | + | __TOC__ |
| - | [[Category: Schwieters, C D | + | </StructureSection> |
| + | [[Category: Bax, A]] | ||
| + | [[Category: Lorieau, J L]] | ||
| + | [[Category: Louis, J M]] | ||
| + | [[Category: Schwieters, C D]] | ||
[[Category: Fusion peptide]] | [[Category: Fusion peptide]] | ||
[[Category: G8a mutant]] | [[Category: G8a mutant]] | ||
Revision as of 11:26, 18 December 2014
Conformational ensemble for the G8A mutant of the influenza hemagglutinin fusion peptide
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