4fqr
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ||
==Crystal structure of broadly neutralizing antibody C05 bound to H3 influenza hemagglutinin== | ==Crystal structure of broadly neutralizing antibody C05 bound to H3 influenza hemagglutinin== | ||
| - | <StructureSection load='4fqr' size='340' side='right' caption='[[4fqr]], [[Resolution|resolution]] 4.10Å' scene=''> | + | <StructureSection load='4fqr' size='340' side='right'caption='[[4fqr]], [[Resolution|resolution]] 4.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fqr]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/I68a4 I68a4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fqr]] is a 48 chain structure with sequence from [http://en.wikipedia.org/wiki/I68a4 I68a4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQR 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= | + | </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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fnk|4fnk]], [[4fnl|4fnl]], [[4fp8|4fp8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fnk|4fnk]], [[4fnl|4fnl]], [[4fp8|4fp8]]</td></tr> | ||
| Line 10: | Line 10: | ||
<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=4fqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqr OCA], [http://pdbe.org/4fqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqr RCSB], [http://www.ebi.ac.uk/pdbsum/4fqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqr ProSAT]</span></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=4fqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqr OCA], [http://pdbe.org/4fqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqr RCSB], [http://www.ebi.ac.uk/pdbsum/4fqr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqr ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == 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). | [[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). | ||
| Line 24: | Line 23: | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[Antibody 3D structures|Antibody 3D structures]] |
| - | *[[3D structures | + | *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 31: | Line 30: | ||
</StructureSection> | </StructureSection> | ||
[[Category: I68a4]] | [[Category: I68a4]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ekiert, D C]] | [[Category: Ekiert, D C]] | ||
[[Category: Wilson, I A]] | [[Category: Wilson, I A]] | ||
Revision as of 10:01, 25 December 2019
Crystal structure of broadly neutralizing antibody C05 bound to H3 influenza hemagglutinin
| |||||||||||
