1xop: Difference between revisions

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==NMR structure of G1V mutant of influenza hemagglutinin fusion peptide in DPC micelles at pH 5==
==NMR structure of G1V mutant of influenza hemagglutinin fusion peptide in DPC micelles at pH 5==
<StructureSection load='1xop' size='340' side='right' caption='[[1xop]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
<StructureSection load='1xop' size='340' side='right' caption='[[1xop]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
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<table><tr><td colspan='2'>[[1xop]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XOP FirstGlance]. <br>
<table><tr><td colspan='2'>[[1xop]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XOP FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xoo|1xoo]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xoo|1xoo]]</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=1xop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xop OCA], [http://pdbe.org/1xop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xop RCSB], [http://www.ebi.ac.uk/pdbsum/1xop PDBsum]</span></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=1xop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xop OCA], [http://pdbe.org/1xop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xop RCSB], [http://www.ebi.ac.uk/pdbsum/1xop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xop ProSAT]</span></td></tr>
</table>
</table>
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Revision as of 10:10, 18 April 2018

NMR structure of G1V mutant of influenza hemagglutinin fusion peptide in DPC micelles at pH 5NMR structure of G1V mutant of influenza hemagglutinin fusion peptide in DPC micelles at pH 5

Structural highlights

1xop is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Influenza virus hemagglutinin (HA)-mediated membrane fusion is initiated by a conformational change that releases a V-shaped hydrophobic fusion domain, the fusion peptide, into the lipid bilayer of the target membrane. The most N-terminal residue of this domain, a glycine, is highly conserved and is particularly critical for HA function; G1S and G1V mutant HAs cause hemifusion and abolish fusion, respectively. We have determined the atomic resolution structures of the G1S and G1V mutant fusion domains in membrane environments. G1S forms a V with a disrupted "glycine edge" on its N-terminal arm and G1V adopts a slightly tilted linear helical structure in membranes. Abolishment of the kink in G1V results in reduced hydrophobic penetration of the lipid bilayer and an increased propensity to form beta-structures at the membrane surface. These results underline the functional importance of the kink in the fusion peptide and suggest a structural role for the N-terminal glycine ridge in viral membrane fusion.

Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.,Li Y, Han X, Lai AL, Bushweller JH, Cafiso DS, Tamm LK J Virol. 2005 Sep;79(18):12065-76. PMID:16140782[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Li Y, Han X, Lai AL, Bushweller JH, Cafiso DS, Tamm LK. Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion. J Virol. 2005 Sep;79(18):12065-76. PMID:16140782 doi:http://dx.doi.org/79/18/12065
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