6n5e: Difference between revisions

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 <StructureSection load='6n5e' size='340' side='right'caption='[[6n5e]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6n5e]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/9infa 9infa] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N5E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N5E FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6n5e]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus Influenza A virus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N5E 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&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11320 9INFA])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6n5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5e OCA], [http://pdbe.org/6n5e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n5e RCSB], [http://www.ebi.ac.uk/pdbsum/6n5e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5e ProSAT]</span></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=6n5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5e OCA], [https://pdbe.org/6n5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n5e RCSB], [https://www.ebi.ac.uk/pdbsum/6n5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5e ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0]] 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.
+[https://www.uniprot.org/uniprot/HEMA_I68A0 HEMA_I68A0] 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 ==See Also==
+*[[Antibody 3D structures|Antibody 3D structures]]
 *[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
@@ Line 26: / Line 27: @@
 __TOC__
 </StructureSection>
+[[Category: Influenza A virus]]
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Bajic, G]]
+[[Category: Bajic G]]
-[[Category: Schmidt, A G]]
+[[Category: Schmidt AG]]
-[[Category: Antibody]]
-[[Category: Complex]]
-[[Category: Glycan]]
-[[Category: Hemagglutinin]]
-[[Category: Immunogen design]]
-[[Category: Influenza]]
-[[Category: Viral protein-immune system complex]]