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Current revision (08:03, 11 January 2023) (edit) (undo)
 
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<StructureSection load='1htm' size='340' side='right'caption='[[1htm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1htm' size='340' side='right'caption='[[1htm]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1htm]] is a 6 chain structure. The April 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hemagglutinin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_4 10.2210/rcsb_pdb/mom_2006_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1htm]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_beta_proteobacterium_UMTRA-608 Uncultured beta proteobacterium UMTRA-608]. The April 2006 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Hemagglutinin'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2006_4 10.2210/rcsb_pdb/mom_2006_4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTM 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=1htm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htm OCA], [https://pdbe.org/1htm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htm RCSB], [https://www.ebi.ac.uk/pdbsum/1htm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htm ProSAT]</span></td></tr>
</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=1htm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htm OCA], [https://pdbe.org/1htm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htm RCSB], [https://www.ebi.ac.uk/pdbsum/1htm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htm ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0]] 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.
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[https://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0] 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Bullough, P A]]
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[[Category: Uncultured beta proteobacterium UMTRA-608]]
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[[Category: Hughson, F M]]
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[[Category: Bullough PA]]
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[[Category: Skehel, J J]]
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[[Category: Hughson FM]]
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[[Category: Wiley, D C]]
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[[Category: Skehel JJ]]
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[[Category: Influenza virus hemagglutinin]]
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[[Category: Wiley DC]]
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[[Category: Viral protein]]
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Current revision

STRUCTURE OF INFLUENZA HAEMAGGLUTININ AT THE PH OF MEMBRANE FUSION

PDB ID 1htm

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