2dci

From Proteopedia

(Difference between revisions)

Current revision

NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5

Structural highlights

2dci is a 1 chain structure with sequence from Influenza A virus (A/swine/Hong Kong/126/1982(H3N2)). 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

HEMA_I82A4 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.

Publication Abstract from PubMed

The fusion peptide of influenza hemagglutinin is crucial for cell entry of this virus. Previous studies showed that this peptide adopts a boomerang-shaped structure in lipid model membranes at the pH of membrane fusion. To examine the role of the boomerang in fusion, we changed several residues proposed to stabilize the kink in this structure and measured fusion. Among these, mutants E11A and W14A expressed hemagglutinins with hemifusion and no fusion activities, and F9A and N12A had no effect on fusion, respectively. Binding enthalpies and free energies of mutant peptides to model membranes and their ability to perturb lipid bilayer structures correlated well with the fusion activities of the parent full-length molecules. The structure of W14A determined by NMR and site-directed spin labeling features a flexible kink that points out of the membrane, in sharp contrast to the more ordered boomerang of the wild-type, which points into the membrane. A specific fixed angle boomerang structure is thus required to support membrane fusion.

Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity.,Lai AL, Park H, White JM, Tamm LK J Biol Chem. 2006 Mar 3;281(9):5760-70. Epub 2005 Dec 28. PMID:16407195^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lai AL, Park H, White JM, Tamm LK. Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity. J Biol Chem. 2006 Mar 3;281(9):5760-70. Epub 2005 Dec 28. PMID:16407195 doi:M512280200

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2dci"

Categories: Large Structures | Lai AL | Tamm LK

@@ Line 1: / Line 1: @@
 ==NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5==
-<StructureSection load='2dci' size='340' side='right'caption='[[2dci]], [[NMR_Ensembles_of_Models | 33 NMR models]]' scene=''>
+<StructureSection load='2dci' size='340' side='right'caption='[[2dci]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2dci]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DCI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2dci]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/swine/Hong_Kong/126/1982(H3N2)) Influenza A virus (A/swine/Hong Kong/126/1982(H3N2))]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DCI FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ibn|1ibn]], [[1ibo|1ibo]], [[1xoo|1xoo]], [[1xop|1xop]]</div></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=2dci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dci OCA], [https://pdbe.org/2dci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dci RCSB], [https://www.ebi.ac.uk/pdbsum/2dci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dci ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/HEMA_I82A4 HEMA_I82A4]] 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.
+[https://www.uniprot.org/uniprot/HEMA_I82A4 HEMA_I82A4] 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;">
 == Publication Abstract from PubMed ==
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lai, A L]]
+[[Category: Lai AL]]
-[[Category: Tamm, L K]]
+[[Category: Tamm LK]]
-[[Category: Fusion peptide]]
-[[Category: Ha]]
-[[Category: Viral protein]]

2dci

From Proteopedia

Current revision

NMR structure of influenza HA fusion peptide mutant W14A in DPC in pH5

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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