4o5i
From Proteopedia
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| - | + | {{Large structure}} | |
| + | {{STRUCTURE_4o5i| PDB=4o5i | SCENE= }} | ||
| + | ===Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin=== | ||
| - | + | ==Function== | |
| + | [[http://www.uniprot.org/uniprot/R9U684_9INFA R9U684_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).[SAAS:SAAS000149_004_327643][RuleBase:RU003324] | ||
| - | + | ==About this Structure== | |
| - | + | [[4o5i]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O5I OCA]. | |
| - | + | [[Category: Lee, P S.]] | |
| + | [[Category: Wilson, I A.]] | ||
| + | [[Category: Immune recognition]] | ||
| + | [[Category: Immunoglobulin]] | ||
| + | [[Category: Viral protein-immune system complex]] | ||
| + | [[Category: Virus attachment and entry]] | ||
Revision as of 10:08, 16 April 2014
Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin
Function
[R9U684_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).[SAAS:SAAS000149_004_327643][RuleBase:RU003324]
About this Structure
4o5i is a 24 chain structure. Full crystallographic information is available from OCA.
