4bsh: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_4bsh|  PDB=4bsh  |  SCENE=  }}
===H7N3 Avian Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue 6'-SLN===
{{ABSTRACT_PUBMED_23787694}}


The entry 4bsh is ON HOLD  until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/Q6GYW3_9INFA Q6GYW3_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:SAAS013829_004_327643]


Authors: Xiong, X., Haire, L.F., Martin, S.R., Wharton, S.A., Daniels, R.S., Bennett, M.S., McCauley, J.W., Collins, P.J., Walker, P.A., Skehel, J.J., Gamblin, S.J.
==About this Structure==
[[4bsh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/turkey/italy/214845/2002(h7n3)) Influenza a virus (a/turkey/italy/214845/2002(h7n3))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BSH OCA].  


Description: H7N3 Avian Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue 6'-SLN
==Reference==
<ref group="xtra">PMID:023787694</ref><references group="xtra"/><references/>
[[Category: Bennett, M S.]]
[[Category: Collins, P J.]]
[[Category: Daniels, R S.]]
[[Category: Gamblin, S J.]]
[[Category: Haire, L F.]]
[[Category: Martin, S R.]]
[[Category: McCauley, J W.]]
[[Category: Skehel, J J.]]
[[Category: Walker, P A.]]
[[Category: Wharton, S A.]]
[[Category: Xiong, X.]]
[[Category: 3sln]]
[[Category: 6sln]]
[[Category: Bird flu]]
[[Category: Fowl plague virus]]
[[Category: Glycoprotein]]
[[Category: Glycosylation]]
[[Category: H5n1]]
[[Category: H7n3]]
[[Category: H7n9]]
[[Category: Lstc]]
[[Category: Pandemic]]
[[Category: Sialyllactosamine]]
[[Category: Viral protein]]
[[Category: Virus receptor]]

Revision as of 17:09, 3 July 2013

Template:STRUCTURE 4bsh

H7N3 Avian Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue 6'-SLNH7N3 Avian Influenza Virus Haemagglutinin in Complex with Human Receptor Analogue 6'-SLN

Template:ABSTRACT PUBMED 23787694

FunctionFunction

[Q6GYW3_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:SAAS013829_004_327643]

About this StructureAbout this Structure

4bsh is a 2 chain structure with sequence from Influenza a virus (a/turkey/italy/214845/2002(h7n3)). Full crystallographic information is available from OCA.

ReferenceReference

[xtra 1]

  1. Xiong X, Martin SR, Haire LF, Wharton SA, Daniels RS, Bennett MS, McCauley JW, Collins PJ, Walker PA, Skehel JJ, Gamblin SJ. Receptor binding by an H7N9 influenza virus from humans. Nature. 2013 Jun 20. doi: 10.1038/nature12372. PMID:23787694 doi:10.1038/nature12372

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