4n61

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'''Unreleased structure'''
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{{STRUCTURE_4n61| PDB=4n61 | SCENE= }}
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===Crystal structure of hemagglutinin from an H7N9 influenza virus in complex with LSTa, extended soaking===
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{{ABSTRACT_PUBMED_24311689}}
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The entry 4n61 is ON HOLD until Paper Publication
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==Function==
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[[http://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]
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Authors: Xu, R., Wilson, I.A.
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==About this Structure==
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[[4n61]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N61 OCA].
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Description: Crystal structure of hemagglutinin from an H7N9 influenza virus in complex with LSTa, extended soaking
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==Reference==
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<ref group="xtra">PMID:024311689</ref><references group="xtra"/><references/>
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[[Category: Wilson, I A.]]
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[[Category: Xu, R.]]
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[[Category: Hemagglutinin]]
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[[Category: Viral envelope protein]]
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[[Category: Viral fusion protein]]
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[[Category: Viral protein]]

Revision as of 10:19, 18 December 2013

Template:STRUCTURE 4n61

Contents

Crystal structure of hemagglutinin from an H7N9 influenza virus in complex with LSTa, extended soaking

Template:ABSTRACT PUBMED 24311689

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]

About this Structure

4n61 is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Xu R, de Vries RP, Zhu X, Nycholat CM, McBride R, Yu W, Paulson JC, Wilson IA. Preferential recognition of avian-like receptors in human influenza A H7N9 viruses. Science. 2013 Dec 6;342(6163):1230-5. doi: 10.1126/science.1243761. PMID:24311689 doi:http://dx.doi.org/10.1126/science.1243761

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OCA

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