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3zp2

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Revision as of 20:22, 4 August 2016

INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTa

Structural highlights

3zp2 is a 2 chain structure with sequence from 9infa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	3zp0, 3zp1, 3zp3, 3zp6, 3zpa, 3zpb
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q6DQ34_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

As avian influenza A(H5N1) viruses continue to circulate in Asia and Africa, global concerns of an imminent pandemic persist. Recent experimental studies suggest that efficient transmission between humans of current H5N1 viruses only requires a few genetic changes. An essential step is alteration of the virus hemagglutinin from preferential binding to avian receptors for the recognition of human receptors present in the upper airway. We have identified receptor-binding changes which emerged during H5N1 infection of humans, due to single amino acid substitutions, Ala134Val and Ile151Phe, in the hemagglutinin. Detailed biological, receptor-binding, and structural analyses revealed reduced binding of the mutated viruses to avian-like receptors, but without commensurate increased binding to the human-like receptors investigated, possibly reflecting a receptor-binding phenotype intermediate in adaptation to more human-like characteristics. These observations emphasize that evolution in nature of avian H5N1 viruses to efficient binding of human receptors is a complex multistep process.

Changes in the hemagglutinin of H5N1 viruses during human infection - Influence on receptor binding.,Crusat M, Liu J, Palma AS, Childs RA, Liu Y, Wharton SA, Lin YP, Coombs PJ, Martin SR, Matrosovich M, Chen Z, Stevens DJ, Hien VM, Thanh TT, Nhu LN, Nguyet LA, Ha DQ, van Doorn HR, Hien TT, Conradt HS, Kiso M, Gamblin SJ, Chai W, Skehel JJ, Hay AJ, Farrar J, de Jong MD, Feizi T Virology. 2013 Sep 17. pii: S0042-6822(13)00481-9. doi:, 10.1016/j.virol.2013.08.010. PMID:24050651^[1]

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

References

↑ Crusat M, Liu J, Palma AS, Childs RA, Liu Y, Wharton SA, Lin YP, Coombs PJ, Martin SR, Matrosovich M, Chen Z, Stevens DJ, Hien VM, Thanh TT, Nhu LN, Nguyet LA, Ha DQ, van Doorn HR, Hien TT, Conradt HS, Kiso M, Gamblin SJ, Chai W, Skehel JJ, Hay AJ, Farrar J, de Jong MD, Feizi T. Changes in the hemagglutinin of H5N1 viruses during human infection - Influence on receptor binding. Virology. 2013 Sep 17. pii: S0042-6822(13)00481-9. doi:, 10.1016/j.virol.2013.08.010. PMID:24050651 doi:10.1016/j.virol.2013.08.010

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/3zp2"

Categories: Gamblin, S J | Liu, J | Skehel, J J | Stevens, D J | Viral protein

@@ Line 1: / Line 1: @@
 ==INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTa==
 <StructureSection load='3zp2' size='340' side='right' caption='[[3zp2]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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">[[3zp0|3zp0]], [[3zp1|3zp1]], [[3zp3|3zp3]], [[3zp6|3zp6]], [[3zpa|3zpa]], [[3zpb|3zpb]]</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=3zp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zp2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zp2 RCSB], [http://www.ebi.ac.uk/pdbsum/3zp2 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=3zp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zp2 OCA], [http://pdbe.org/3zp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zp2 RCSB], [http://www.ebi.ac.uk/pdbsum/3zp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zp2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3zp2" style="background-color:#fffaf0;"></div>
 ==See Also==

3zp2

From Proteopedia

Revision as of 20:22, 4 August 2016

INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTa

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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