4nkj

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'''Unreleased structure'''
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{{STRUCTURE_4nkj| PDB=4nkj | SCENE= }}
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===Structure of influenza B virus hemagglutinin at membrane fusion pH===
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{{ABSTRACT_PUBMED_24433110}}
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The entry 4nkj is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/S5DRP1_9INFB S5DRP1_9INFB]] 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]
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Authors: Ni, F., Chen, X., Shen, J., Wang, Q.
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==About this Structure==
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[[4nkj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NKJ OCA].
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Description: Structure of influenza B virus hemagglutinin at membrane fusion pH
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==Reference==
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<ref group="xtra">PMID:024433110</ref><references group="xtra"/><references/>
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[[Category: Chen, X.]]
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[[Category: Ni, F.]]
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[[Category: Shen, J.]]
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[[Category: Wang, Q.]]
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[[Category: Ha]]
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[[Category: Viral protein]]

Revision as of 09:21, 2 April 2014

Template:STRUCTURE 4nkj

Contents

Structure of influenza B virus hemagglutinin at membrane fusion pH

Template:ABSTRACT PUBMED 24433110

Function

[S5DRP1_9INFB] 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]

About this Structure

4nkj is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Ni F, Chen X, Shen J, Wang Q. Structural insights into the membrane fusion mechanism mediated by influenza virus hemagglutinin. Biochemistry. 2014 Feb 11;53(5):846-54. doi: 10.1021/bi401525h. Epub 2014 Jan 28. PMID:24433110 doi:http://dx.doi.org/10.1021/bi401525h

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OCA

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