3whe

From Proteopedia

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'''Unreleased structure'''
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{{Large structure}}
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{{STRUCTURE_3whe| PDB=3whe | SCENE= }}
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===A new conserved neutralizing epitope at the globular head of hemagglutinin in H3N2 influenza viruses===
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{{ABSTRACT_PUBMED_24719430}}
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The entry 3whe is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/T2HNI1_9INFA T2HNI1_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:SAAS000149_004_327643]
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Authors: Fujii, Y., Sumida, T., Shirouzu, M., Yokoyama, S.
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==About this Structure==
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[[3whe]] is a 36 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHE OCA].
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Description: A new conserved neutralizing epitope at the globular head of hemagglutinin in H3N2 influenza viruses
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==Reference==
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<ref group="xtra">PMID:024719430</ref><references group="xtra"/><references/>
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[[Category: Fujii, Y.]]
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[[Category: Shirouzu, M.]]
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[[Category: Sumida, T.]]
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[[Category: Yokoyama, S.]]
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[[Category: Viral protein-immune system complex]]

Revision as of 07:44, 23 April 2014

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Template:STRUCTURE 3whe

Contents

A new conserved neutralizing epitope at the globular head of hemagglutinin in H3N2 influenza viruses

Template:ABSTRACT PUBMED 24719430

Function

[T2HNI1_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:SAAS000149_004_327643]

About this Structure

3whe is a 36 chain structure. Full crystallographic information is available from OCA.

Reference

  • Iba Y, Fujii Y, Ohshima N, Sumida T, Kubota-Koketsu R, Ikeda M, Wakiyama M, Shirouzu M, Okada J, Okuno Y, Kurosawa Y, Yokoyama S. Conserved Neutralizing Epitope at Globular Head of Hemagglutinin in H3N2 Influenza Viruses. J Virol. 2014 Apr 9. PMID:24719430 doi:http://dx.doi.org/10.1128/JVI.00420-14

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OCA

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