4o5i: Difference between revisions

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~~'''Unreleased~~ structure~~'''~~

===Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin===

~~The entry 4o5i is ON HOLD until Paper Publication~~

==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]

~~Authors~~: Lee, P.S., Wilson, I.A.

==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].

~~Description~~: ~~Crystal structure of broadly neutralizing antibody F045~~-~~092 in~~ complex ~~with A/Victoria/361/2011 (H3N2) influenza hemagglutinin~~

[[Category: Lee, P S.]]

[[Category: Wilson, I A.]]

[[Category: Immune recognition]]

[[Category: Immunoglobulin]]

[[Category: Viral protein-immune system complex]]

[[Category: Virus attachment and entry]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{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===
-The entry 4o5i is ON HOLD  until Paper Publication
+==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]
-Authors: Lee, P.S., Wilson, I.A.
+==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].
-Description: Crystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin
+[[Category: Lee, P S.]]
+[[Category: Wilson, I A.]]
+[[Category: Immune recognition]]
+[[Category: Immunoglobulin]]
+[[Category: Viral protein-immune system complex]]
+[[Category: Virus attachment and entry]]