We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

4we6

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:03, 7 April 2023

The crystal structure of hemagglutinin HA1 domain from influenza virus A/Perth/142/2007(H3N2)

Structural highlights

4we6 is a 2 chain structure with sequence from Influenza A virus (A/Perth/142/2007(H3N2)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B2VNP1_9INFA 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.[RuleBase:RU003324]

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/4we6"

@@ Line 1: / Line 1: @@
 ==The crystal structure of hemagglutinin HA1 domain from influenza virus A/Perth/142/2007(H3N2)==
-<StructureSection load='4we6' size='340' side='right' caption='[[4we6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='4we6' size='340' side='right'caption='[[4we6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4we6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/perth/142/2007(h3n2)) Influenza a virus (a/perth/142/2007(h3n2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4we6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Perth/142/2007(H3N2)) Influenza A virus (A/Perth/142/2007(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WE6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we5|4we5]], [[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'>[https://proteopedia.org/fgij/fg.htm?mol=4we6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we6 OCA], [https://pdbe.org/4we6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4we6 RCSB], [https://www.ebi.ac.uk/pdbsum/4we6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4we6 ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=529795 Influenza A virus (A/Perth/142/2007(H3N2))])</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=4we6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we6 OCA], [http://pdbe.org/4we6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we6 RCSB], [http://www.ebi.ac.uk/pdbsum/4we6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/G8HJ45_9INFA G8HJ45_9INFA]] 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.[RuleBase:RU003324][SAAS:SAAS00145386]
+[https://www.uniprot.org/uniprot/B2VNP1_9INFA B2VNP1_9INFA] 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.[RuleBase:RU003324]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Carney, P J]]
+[[Category: Large Structures]]
-[[Category: Chang, J C]]
+[[Category: Carney PJ]]
-[[Category: Guo, Z]]
+[[Category: Chang JC]]
-[[Category: Stevens, J]]
+[[Category: Guo Z]]
-[[Category: Villanueva, J M]]
+[[Category: Stevens J]]
-[[Category: Yang, H]]
+[[Category: Villanueva JM]]
-[[Category: H3n2]]
+[[Category: Yang H]]
-[[Category: Ha1]]
-[[Category: Hemagglutinin]]
-[[Category: Influenza virus]]
-[[Category: Viral protein]]

4we6

From Proteopedia

Revision as of 07:03, 7 April 2023

The crystal structure of hemagglutinin HA1 domain from influenza virus A/Perth/142/2007(H3N2)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox