6ii8: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ii8 is ON HOLD
+==Crystal structure of H7 hemagglutinin from A/Anhui/1/2013 in complex with a human neutralizing antibody L4B-18==
+<StructureSection load='6ii8' size='340' side='right' caption='[[6ii8]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
-Authors: Huang, K.Y., Rijal, P., Jiang, H.H., Wang, B.B., Schimanski, L., Dong, T., Liu, Y.M., Chang, P.X., Iqbal, M., Wang, M.C., Chen, Z.H., Song, R., Huang, C.C., Yang, J.H., Qi, J.X., Lin, T.Y., Li, A., Powell, T.J., Ma, C., Jan, J.T., Gao, G.F., Shi, Y., Townsend, A.R.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ii8]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6II8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6II8 FirstGlance]. <br>
-Description: Structure-function Analysis of Neutralizing Antibodies to H7N9 influenza from Naturally Infected Humans
+</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>
-[[Category: Unreleased Structures]]
+<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=6ii8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ii8 OCA], [http://pdbe.org/6ii8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ii8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ii8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ii8 ProSAT]</span></td></tr>
-[[Category: Qi, J.X]]
+</table>
-[[Category: Gao, G.F]]
+== Function ==
-[[Category: Jiang, H.H]]
+[[http://www.uniprot.org/uniprot/A0A024CX39_9INFA A0A024CX39_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 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.[HAMAP-Rule:MF_04072][SAAS:SAAS01039073]  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] [[http://www.uniprot.org/uniprot/A0A0K1LUI9_9INFA A0A0K1LUI9_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 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.[HAMAP-Rule:MF_04072][SAAS:SAAS01039073]  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]
-[[Category: Wang, B.B]]
+__TOC__
-[[Category: Powell, T.J]]
+</StructureSection>
-[[Category: Rijal, P]]
+[[Category: Gao, G F]]
-[[Category: Wang, M.C]]
+[[Category: Jiang, H H]]
-[[Category: Schimanski, L]]
+[[Category: Qi, J]]
-[[Category: Yang, J.H]]
-[[Category: Huang, K.Y]]
-[[Category: Ma, C]]
-[[Category: Townsend, A.R]]
-[[Category: Chang, P.X]]
-[[Category: Li, A]]
-[[Category: Chen, Z.H]]
-[[Category: Dong, T]]
-[[Category: Lin, T.Y]]
 [[Category: Shi, Y]]
-[[Category: Jan, J.T]]
+[[Category: H7 haemagglutinin]]
-[[Category: Song, R]]
+[[Category: Immune system]]
-[[Category: Liu, Y.M]]
+[[Category: Neutralizing antibody]]
-[[Category: Iqbal, M]]
+[[Category: Protection in vivo]]
-[[Category: Huang, C.C]]
+[[Category: Receptor binding site]]