1ibo: Difference between revisions

Revision as of 14:10, 21 February 2008

NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4

OverviewOverview

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.

About this StructureAbout this Structure

1IBO is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 13:10:05 2008

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OCA

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-[[Image:1ibo.gif|left|200px]]<br /><applet load="1ibo" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ibo.gif|left|200px]]<br /><applet load="1ibo" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ibo" />
 '''NMR STRUCTURE OF HEMAGGLUTININ FUSION PEPTIDE IN DPC MICELLES AT PH 7.4'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-IBO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IBO OCA].
+IBO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IBO OCA].
 ==Reference==
 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11473264 11473264]
 [[Category: Single protein]]
-[[Category: Bushweller, J.H.]]
+[[Category: Bushweller, J H.]]
-[[Category: Cafiso, D.S.]]
+[[Category: Cafiso, D S.]]
 [[Category: Han, X.]]
-[[Category: Tamm, L.K.]]
+[[Category: Tamm, L K.]]
 [[Category: helix-kink-irregular]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:15:54 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:05 2008''