4ln3

From Proteopedia

(Difference between revisions)

Current revision

The crystal structure of hemagglutinin from a H7N9 influenza virus (A/Shanghai/1/2013)

Structural highlights

4ln3 is a 12 chain structure with sequence from Influenza A virus (A/Shanghai/02/2013(H7N9)). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.65Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

R4NN21_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]

Publication Abstract from PubMed

In March 2013, the Chinese Centers for Disease Control and Prevention reported human infections with an H7N9 influenza virus, and by July 20th 2013, the numbers of laboratory-confirmed cases had climbed to 134, including 43 fatalities and 127 hospitalizations. The newly emerging H7N9 viruses constitute an obvious public health concern because of the apparent severity of this outbreak. Here we focus on the hemagglutinin (HA) of these viruses and assess its receptor binding phenotype in relation to previous HAs studied. Glycan microarray and kinetic analysis of recombinant A(H7N9) HAs was performed to compare the receptor binding profile of wild-type receptor binding site variants, at position 217, a residue analogous to one of two positions known to switch avian to human receptor preference in H2N2 and H3N2 viruses. Two recombinant A(H7N9) HAs were structurally characterized and a mutational study of the receptor binding site was performed to analyze important residues that can affect receptor preference and affinity. Results highlight a weak human receptor preference of the H7N9 HAs suggesting that these viruses require further adaptation in order to adapt fully to humans.

Structural analysis of the hemagglutinin from the recent 2013 H7N9 influenza virus.,Yang H, Carney PJ, Chang JC, Villanueva JM, Stevens J J Virol. 2013 Sep 11. PMID:24027325^[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. Structural analysis of the hemagglutinin from the recent 2013 H7N9 influenza virus. J Virol. 2013 Sep 11. PMID:24027325 doi:10.1128/JVI.01854-13

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/4ln3"

@@ Line 3: / Line 3: @@
 <StructureSection load='4ln3' size='340' side='right'caption='[[4ln3]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ln3]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/shanghai/02/2013(h7n9)) Influenza a virus (a/shanghai/02/2013(h7n9))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LN3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ln3]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Shanghai/02/2013(H7N9)) Influenza A virus (A/Shanghai/02/2013(H7N9))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LN3 FirstGlance]. <br>
-</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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kth|4kth]], [[4kw1|4kw1]], [[4kwm|4kwm]], [[4ln4|4ln4]], [[4ln6|4ln6]], [[4ln8|4ln8]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4ln3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ln3 OCA], [http://pdbe.org/4ln3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ln3 RCSB], [http://www.ebi.ac.uk/pdbsum/4ln3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ln3 ProSAT]</span></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=4ln3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ln3 OCA], [https://pdbe.org/4ln3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ln3 RCSB], [https://www.ebi.ac.uk/pdbsum/4ln3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ln3 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/R4NN21_9INFA R4NN21_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 (By similarity).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 21: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
@@ Line 25: / Line 27: @@
 </StructureSection>
 [[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: Receptor specificity]]
-[[Category: Viral protein]]

4ln3

From Proteopedia

Current revision

The crystal structure of hemagglutinin from a H7N9 influenza virus (A/Shanghai/1/2013)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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