5y2m

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:20, 22 November 2023) (edit) (undo)
 
Line 1: Line 1:
==Crystal structure of a group 2 HA binding antibody AF4H1K1 Fab in complex with the H4N6 duck isolate (H4-CZ/56) hemagglutinin==
==Crystal structure of a group 2 HA binding antibody AF4H1K1 Fab in complex with the H4N6 duck isolate (H4-CZ/56) hemagglutinin==
-
<StructureSection load='5y2m' size='340' side='right' caption='[[5y2m]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+
<StructureSection load='5y2m' size='340' side='right'caption='[[5y2m]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5y2m]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y2M FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5y2m]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/duck/Czechoslovakia/1956(H4N6)) Influenza A virus (A/duck/Czechoslovakia/1956(H4N6))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y2M FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</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=5y2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2m OCA], [http://pdbe.org/5y2m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y2m RCSB], [http://www.ebi.ac.uk/pdbsum/5y2m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2m ProSAT]</span></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y2m OCA], [https://pdbe.org/5y2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y2m RCSB], [https://www.ebi.ac.uk/pdbsum/5y2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y2m ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/A3KF09_I56A1 A3KF09_I56A1]] 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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS00842036] 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.[RuleBase:RU003324]
+
[https://www.uniprot.org/uniprot/A3KF09_I56A1 A3KF09_I56A1] 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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS00842036] 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.[RuleBase:RU003324]
 +
 
 +
==See Also==
 +
*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Gao, F G]]
+
[[Category: Homo sapiens]]
-
[[Category: Qi, J]]
+
[[Category: Large Structures]]
-
[[Category: Xiao, H]]
+
[[Category: Gao FG]]
-
[[Category: H3-clade]]
+
[[Category: Qi J]]
-
[[Category: Ha]]
+
[[Category: Xiao H]]
-
[[Category: Immune system]]
+
-
[[Category: Influenza virus]]
+
-
[[Category: Neutralizing antibody]]
+

Current revision

Crystal structure of a group 2 HA binding antibody AF4H1K1 Fab in complex with the H4N6 duck isolate (H4-CZ/56) hemagglutinin

PDB ID 5y2m

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools