4lxv

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'''Unreleased structure'''
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{{STRUCTURE_4lxv| PDB=4lxv | SCENE= }}
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===Crystal Structure of the Hemagglutinin from a H1N1pdm A/WASHINGTON/5/2011 virus===
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{{ABSTRACT_PUBMED_24522930}}
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The entry 4lxv is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/J7MFR5_9INFA J7MFR5_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:SAAS001364_004_327643]
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Authors: Yang, H., Chang, J.C., Guo, Z., Carney, P.J., Shore, D.A., Donis, R.O., Cox, N.J., Villanueva, J.M., Klimov, A.I., Stevens, J.
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==About this Structure==
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[[4lxv]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LXV OCA].
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Description: Crystal Structure of the Hemagglutinin from a H1N1pdm A/WASHINGTON/5/2011 virus
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==Reference==
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<ref group="xtra">PMID:024522930</ref><references group="xtra"/><references/>
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[[Category: Carney, P J.]]
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[[Category: Chang, J C.]]
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[[Category: Cox, N J.]]
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[[Category: Donis, R O.]]
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[[Category: Guo, Z.]]
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[[Category: Klimov, A I.]]
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[[Category: Shore, D A.]]
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[[Category: Stevens, J.]]
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[[Category: Villanueva, J M.]]
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[[Category: Yang, H.]]
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[[Category: Hemagglutinin]]
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[[Category: Influenza]]
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[[Category: Pandemic]]
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[[Category: Viral protein]]

Revision as of 18:04, 3 March 2014

Template:STRUCTURE 4lxv

Contents

Crystal Structure of the Hemagglutinin from a H1N1pdm A/WASHINGTON/5/2011 virus

Template:ABSTRACT PUBMED 24522930

Function

[J7MFR5_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:SAAS001364_004_327643]

About this Structure

4lxv is a 12 chain structure. Full crystallographic information is available from OCA.

Reference

  • Yang H, Chang JC, Guo Z, Carney PJ, Shore DA, Donis RO, Cox NJ, Villanueva JM, Klimov AI, Stevens J. Structural stability of influenza A(H1N1)pdm09 virus hemagglutinins. J Virol. 2014 Feb 12. PMID:24522930 doi:http://dx.doi.org/10.1128/JVI.02278-13

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OCA

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