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==The hemagglutinin fusion peptide (H1 subtype) at pH 7.4==
==The hemagglutinin fusion peptide (H1 subtype) at pH 7.4==
<StructureSection load='2kxa' size='340' side='right'caption='[[2kxa]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2kxa' size='340' side='right'caption='[[2kxa]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2kxa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/swine/scotland/410440/94_(h1n2)) Influenza a virus (a/swine/scotland/410440/94 (h1n2))]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXA FirstGlance]. <br>
<table><tr><td colspan='2'>[[2kxa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Scotland/410440/94(H1N2)) Influenza A virus (A/swine/Scotland/410440/94(H1N2))]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXA FirstGlance]. <br>
</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=2kxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxa OCA], [https://pdbe.org/2kxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxa RCSB], [https://www.ebi.ac.uk/pdbsum/2kxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxa ProSAT]</span></td></tr>
</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=2kxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxa OCA], [https://pdbe.org/2kxa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxa RCSB], [https://www.ebi.ac.uk/pdbsum/2kxa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxa ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q9YTC2_9INFA Q9YTC2_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][SAAS:SAAS00046902]  
[https://www.uniprot.org/uniprot/Q9YTC2_9INFA Q9YTC2_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][SAAS:SAAS00046902]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
All but five of the N-terminal 23 residues of the HA2 domain of the influenza virus glycoprotein hemagglutinin (HA) are strictly conserved across all 16 serotypes of HA genes. The structure and function of this HA2 fusion peptide (HAfp) continues to be the focus of extensive biophysical, computational, and functional analysis, but most of these analyses are of peptides that do not include the strictly conserved residues Trp(21)-Tyr(22)-Gly(23). The heteronuclear triple resonance NMR study reported here of full length HAfp of sero subtype H1, solubilized in dodecylphosphatidyl choline, reveals a remarkably tight helical hairpin structure, with its N-terminal alpha-helix (Gly(1)-Gly(12)) packed tightly against its second alpha-helix (Trp(14)-Gly(23)), with six of the seven conserved Gly residues at the interhelical interface. The seventh conserved Gly residue in position 13 adopts a positive angle, enabling the hairpin turn that links the two helices. The structure is stabilized by multiple interhelical C(alpha)H to C = O hydrogen bonds, characterized by strong interhelical H(N)-H(alpha) and H(alpha)-H(alpha) NOE contacts. Many of the previously identified mutations that make HA2 nonfusogenic are also incompatible with the tight antiparallel hairpin arrangement of the HAfp helices.(15)N relaxation analysis indicates the structure to be highly ordered on the nanosecond time scale, and NOE analysis indicates HAfp is located at the water-lipid interface, with its hydrophobic surface facing the lipid environment, and the Gly-rich side of the helix-helix interface exposed to solvent.
 
The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface.,Lorieau JL, Louis JM, Bax A Proc Natl Acad Sci U S A. 2010 Jun 2. PMID:20534508<ref>PMID:20534508</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2kxa" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bax, A]]
[[Category: Bax A]]
[[Category: Lorieau, J L]]
[[Category: Lorieau JL]]
[[Category: Louis, J M]]
[[Category: Louis JM]]
[[Category: Fusion peptide]]
[[Category: Immune system]]
[[Category: Influenza]]
[[Category: Viral protein]]

Latest revision as of 09:49, 1 May 2024

The hemagglutinin fusion peptide (H1 subtype) at pH 7.4The hemagglutinin fusion peptide (H1 subtype) at pH 7.4

Structural highlights

2kxa is a 1 chain structure with sequence from Influenza A virus (A/swine/Scotland/410440/94(H1N2)). Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9YTC2_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][SAAS:SAAS00046902]

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