1ibo: Difference between revisions
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==NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4== | |||
<StructureSection load='1ibo' size='340' side='right' caption='[[1ibo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ibo]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IBO FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ibn|1ibn]]</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=1ibo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ibo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ibo RCSB], [http://www.ebi.ac.uk/pdbsum/1ibo PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The N-terminal domain of the influenza hemagglutinin (HA) is the only portion of the molecule that inserts deeply into membranes of infected cells to mediate the viral and the host cell membrane fusion. This domain constitutes an autonomous folding unit in the membrane, causes hemolysis of red blood cells and catalyzes lipid exchange between juxtaposed membranes in a pH-dependent manner. Combining NMR structures determined at pHs 7.4 and 5 with EPR distance constraints, we have deduced the structures of the N-terminal domain of HA in the lipid bilayer. At both pHs, the domain is a kinked, predominantly helical amphipathic structure. At the fusogenic pH 5, however, the domain has a sharper bend, an additional 3(10)-helix and a twist, resulting in the repositioning of Glu 15 and Asp 19 relative to that at the nonfusogenic pH 7.4. Rotation of these charged residues out of the membrane plane creates a hydrophobic pocket that allows a deeper insertion of the fusion domain into the core of the lipid bilayer. Such an insertion mode could perturb lipid packing and facilitate lipid mixing between juxtaposed membranes. | |||
Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin.,Han X, Bushweller JH, Cafiso DS, Tamm LK Nat Struct Biol. 2001 Aug;8(8):715-20. PMID:11473264<ref>PMID:11473264</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hemagglutinin|Hemagglutinin]] | *[[Hemagglutinin|Hemagglutinin]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Bushweller, J H | </StructureSection> | ||
[[Category: Cafiso, D S | [[Category: Bushweller, J H]] | ||
[[Category: Han, X | [[Category: Cafiso, D S]] | ||
[[Category: Tamm, L K | [[Category: Han, X]] | ||
[[Category: Tamm, L K]] | |||
[[Category: Helix-kink-irregular]] | [[Category: Helix-kink-irregular]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 17:10, 17 December 2014
NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4
Structural highlights
Publication Abstract from PubMedThe N-terminal domain of the influenza hemagglutinin (HA) is the only portion of the molecule that inserts deeply into membranes of infected cells to mediate the viral and the host cell membrane fusion. This domain constitutes an autonomous folding unit in the membrane, causes hemolysis of red blood cells and catalyzes lipid exchange between juxtaposed membranes in a pH-dependent manner. Combining NMR structures determined at pHs 7.4 and 5 with EPR distance constraints, we have deduced the structures of the N-terminal domain of HA in the lipid bilayer. At both pHs, the domain is a kinked, predominantly helical amphipathic structure. At the fusogenic pH 5, however, the domain has a sharper bend, an additional 3(10)-helix and a twist, resulting in the repositioning of Glu 15 and Asp 19 relative to that at the nonfusogenic pH 7.4. Rotation of these charged residues out of the membrane plane creates a hydrophobic pocket that allows a deeper insertion of the fusion domain into the core of the lipid bilayer. Such an insertion mode could perturb lipid packing and facilitate lipid mixing between juxtaposed membranes. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin.,Han X, Bushweller JH, Cafiso DS, Tamm LK Nat Struct Biol. 2001 Aug;8(8):715-20. PMID:11473264[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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