4ubd: Difference between revisions
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''' | ==Crystal structure of a neutralizing human monoclonal antibody with 1968 H3 HA== | ||
<StructureSection load='4ubd' size='340' side='right' caption='[[4ubd]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ubd]] is a 24 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UBD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UBD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ubd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ubd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ubd RCSB], [http://www.ebi.ac.uk/pdbsum/4ubd PDBsum]</span></td></tr> | |||
</table> | |||
[[Category: | == Function == | ||
[[http://www.uniprot.org/uniprot/HEMA_I68A4 HEMA_I68A4]] 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). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cho, M]] | |||
[[Category: Donis, R O]] | |||
[[Category: Shore, D A]] | |||
[[Category: Stevens, J]] | |||
[[Category: Yang, H]] | [[Category: Yang, H]] | ||
[[Category: | [[Category: H3n2]] | ||
[[Category: | [[Category: Hemagglutinin]] | ||
[[Category: | [[Category: Monoclonal antibody]] | ||
[[Category: | [[Category: Viral protein-immune system complex]] | ||
Revision as of 16:00, 24 June 2015
Crystal structure of a neutralizing human monoclonal antibody with 1968 H3 HACrystal structure of a neutralizing human monoclonal antibody with 1968 H3 HA
Structural highlights
Function[HEMA_I68A4] 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). |
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