4we4

From Proteopedia

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Revision as of 00:15, 26 January 2017

The crystal structure of hemagglutinin from 1968 H3N2 influenza virus

Structural highlights

4we4 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , ,
Related:	4we5, 4we6, 4we7, 4we8, 4we9, 4wea
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HEMA_I68A4] 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 (By similarity).

Publication Abstract from PubMed

A(H3N2) influenza viruses have circulated in humans since 1968, and antigenic drift of the hemagglutinin (HA) protein continues to be a driving force that allows the virus to escape the human immune response. Since the major antigenic sites of the HA overlap into the receptor binding site (RBS) of the molecule, the virus constantly struggles to effectively adapt to host immune responses, without compromising its functionality. Here, we have structurally assessed the evolution of the A(H3N2) virus HA RBS, using an established recombinant expression system. Glycan binding specificities of nineteen A(H3N2) influenza virus HAs, each a component of the seasonal influenza vaccine between 1968 and 2012, were analyzed. Results suggest that while its receptor-binding site has evolved from one that can bind a broad range of human receptor analogs to one with a more restricted binding profile for longer glycans, the virus continues to circulate and transmit efficiently among humans.

Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins.,Yang H, Carney PJ, Chang JC, Guo Z, Villanueva JM, Stevens J Virology. 2015 Jan 21;477C:18-31. doi: 10.1016/j.virol.2014.12.024. PMID:25617824^[1]

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

References

↑ Yang H, Carney PJ, Chang JC, Guo Z, Villanueva JM, Stevens J. Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins. Virology. 2015 Jan 21;477C:18-31. doi: 10.1016/j.virol.2014.12.024. PMID:25617824 doi:http://dx.doi.org/10.1016/j.virol.2014.12.024

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/4we4"

@@ Line 1: / Line 1: @@
 ==The crystal structure of hemagglutinin from 1968 H3N2 influenza virus==
 <StructureSection load='4we4' size='340' side='right' caption='[[4we4]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PE5:3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL'>PE5</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we5|4we5]], [[4we6|4we6]], [[4we7|4we7]], [[4we8|4we8]], [[4we9|4we9]], [[4wea|4wea]]</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=4we4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4we4 RCSB], [http://www.ebi.ac.uk/pdbsum/4we4 PDBsum]</span></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=4we4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we4 OCA], [http://pdbe.org/4we4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we4 RCSB], [http://www.ebi.ac.uk/pdbsum/4we4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we4 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4we4" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Hemagglutinin|Hemagglutinin]]
 == References ==
 <references/>

4we4

From Proteopedia

Revision as of 00:15, 26 January 2017

The crystal structure of hemagglutinin from 1968 H3N2 influenza virus

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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