4kvn

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Template:STRUCTURE 4kvn

Contents 1 Crystal structure of Fab 39.29 in complex with Influenza Hemagglutinin A/Perth/16/2009 (H3N2) 2 Function 3 About this Structure 4 Reference

Crystal structure of Fab 39.29 in complex with Influenza Hemagglutinin A/Perth/16/2009 (H3N2)

Template:ABSTRACT PUBMED 23870317

Function

[C6KNH7_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

4kvn is a 3 chain structure with sequence from Homo sapiens and Influenza a virus (a/perth/16/2009(h3n2)). Full crystallographic information is available from OCA.

Reference

• Nakamura G, Chai N, Park S, Chiang N, Lin Z, Chiu H, Fong R, Yan D, Kim J, Zhang J, Lee WP, Estevez A, Coons M, Xu M, Lupardus P, Balazs M, Swem LR. An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza a antibodies. Cell Host Microbe. 2013 Jul 17;14(1):93-103. doi: 10.1016/j.chom.2013.06.004. PMID:23870317 doi:10.1016/j.chom.2013.06.004