4wsu

From Proteopedia

(Difference between revisions)

Revision as of 07:24, 7 April 2023

The crystal structure of hemagglutinin from A/Taiwan/1/2013 in complex with 3'SLN

Structural highlights

4wsu is a 6 chain structure with sequence from Influenza A virus. 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

A0A0J9X246_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

During 2013, three new avian influenza A virus subtypes, A(H7N9), A(H6N1) and A(H10N8), resulted in human infections. While the A(H7N9) virus resulted in a significant epidemic in China across 19 provinces and municipalities, both A(H6N1) and A(H10N8) viruses resulted in only a few human infections. This study focuses on the major surface glycoprotein hemagglutinin from both of these novel human viruses. The detailed structural and glycan microarray analyses presented here highlight that both A(H6N1) and A(H10N8) virus hemagglutinins retain a strong avian receptor binding preference, and thus currently pose a low risk for sustained human infections. IMPORTANCE: Human infections with zoonotic influenza virus subtypes continue to be a great public health concern. We report detailed structural analysis and glycan microarray data for recombinant hemagglutinins from A(H6N1) and A(H10N8) viruses, isolated from human infections in 2013, and compare them with hemagglutinins of avian origin. This is the first structural report of an H6 HA, and our results should further the understanding of these viruses, and provide useful information to aid continuous surveillance of these zoonotic influenza viruses.

Structure and receptor binding preferences of recombinant hemagglutinins from avian and human H6 and H10 influenza A virus subtypes.,Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J J Virol. 2015 Feb 11. pii: JVI.03456-14. PMID:25673707^[1]

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

References

↑ Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J. Structure and receptor binding preferences of recombinant hemagglutinins from avian and human H6 and H10 influenza A virus subtypes. J Virol. 2015 Feb 11. pii: JVI.03456-14. PMID:25673707 doi:http://dx.doi.org/10.1128/JVI.03456-14

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/4wsu"

@@ Line 3: / Line 3: @@
 <StructureSection load='4wsu' size='340' side='right'caption='[[4wsu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4wsu]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/9infa 9infa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WSU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4wsu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WSU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4wsr|4wsr]], [[4wss|4wss]], [[4wst|4wst]], [[4wsv|4wsv]], [[4wsw|4wsw]], [[4wsx|4wsx]]</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=4wsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsu OCA], [https://pdbe.org/4wsu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wsu RCSB], [https://www.ebi.ac.uk/pdbsum/4wsu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsu ProSAT]</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=4wsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wsu OCA], [http://pdbe.org/4wsu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wsu RCSB], [http://www.ebi.ac.uk/pdbsum/4wsu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wsu ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A0A0J9X246_9INFA A0A0J9X246_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 19: / Line 20: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Influenza A virus]]
 [[Category: Large Structures]]
-[[Category: Carney, P J]]
+[[Category: Carney PJ]]
-[[Category: Chang, J C]]
+[[Category: Chang JC]]
-[[Category: Stevens, J]]
+[[Category: Stevens J]]
-[[Category: Villanueva, J M]]
+[[Category: Villanueva JM]]
-[[Category: Yang, H]]
+[[Category: Yang H]]
-[[Category: H6]]
-[[Category: Hemagglutinin]]
-[[Category: Influenza virus]]
-[[Category: Viral protein]]

4wsu

From Proteopedia

Revision as of 07:24, 7 April 2023

The crystal structure of hemagglutinin from A/Taiwan/1/2013 in complex with 3'SLN

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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