3zp3

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Template:STRUCTURE 3zp3

Contents

INFLUENZA VIRUS (VN1194) H5 HA A138V mutant with LSTc

Template:ABSTRACT PUBMED 24050651

Function

[Q6DQ34_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

3zp3 is a 2 chain structure with sequence from Influenza a virus (a/viet nam/1194/2004(h5n1)). Full crystallographic information is available from OCA.

Reference

  • Crusat M, Liu J, Palma AS, Childs RA, Liu Y, Wharton SA, Lin YP, Coombs PJ, Martin SR, Matrosovich M, Chen Z, Stevens DJ, Hien VM, Thanh TT, Nhu LN, Nguyet LA, Ha DQ, van Doorn HR, Hien TT, Conradt HS, Kiso M, Gamblin SJ, Chai W, Skehel JJ, Hay AJ, Farrar J, de Jong MD, Feizi T. Changes in the hemagglutinin of H5N1 viruses during human infection - Influence on receptor binding. Virology. 2013 Sep 17. pii: S0042-6822(13)00481-9. doi:, 10.1016/j.virol.2013.08.010. PMID:24050651 doi:10.1016/j.virol.2013.08.010

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