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==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]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1xop]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Netherlands/284/03(H7N7)) Influenza A virus (A/Netherlands/284/03(H7N7))]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1XOP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution 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=1xop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xop OCA], [https://pdbe.org/1xop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xop RCSB], [https://www.ebi.ac.uk/pdbsum/1xop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xop ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6VMJ8_9INFA Q6VMJ8_9INFA] Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:16140782</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1xop" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] | |||
[[Category: Bushweller | == References == | ||
[[Category: Cafiso | <references/> | ||
[[Category: Han | __TOC__ | ||
[[Category: Lai | </StructureSection> | ||
[[Category: Li | [[Category: Large Structures]] | ||
[[Category: Tamm | [[Category: Bushweller JH]] | ||
[[Category: Cafiso DS]] | |||
[[Category: Han X]] | |||
[[Category: Lai AL]] | |||
[[Category: Li Y]] | |||
[[Category: Tamm LK]] | |||
Latest revision as of 12:29, 6 December 2023
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
FunctionQ6VMJ8_9INFA Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.[RuleBase:RU003324] Publication Abstract from PubMedInfluenza 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 AlsoReferences
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