4jug: Difference between revisions

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 ==Crystal structure of 1918 pandemic influenza virus hemagglutinin mutant D225G==
-<StructureSection load='4jug' size='340' side='right' caption='[[4jug]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='4jug' size='340' side='right'caption='[[4jug]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4jug]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/south_carolina/1/18_(h1n1)) Influenza a virus (a/south carolina/1/18 (h1n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JUG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4jug]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/South_Carolina/1/1918(H1N1)) Influenza A virus (A/South Carolina/1/1918(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JUG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JUG 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></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jtv|4jtv]], [[4jtx|4jtx]], [[4ju0|4ju0]], [[4juh|4juh]], [[4juj|4juj]]</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=4jug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jug OCA], [https://pdbe.org/4jug PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jug RCSB], [https://www.ebi.ac.uk/pdbsum/4jug PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jug ProSAT]</span></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=59375 Influenza A virus (A/South Carolina/1/18 (H1N1))])</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=4jug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jug OCA], [http://pdbe.org/4jug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jug RCSB], [http://www.ebi.ac.uk/pdbsum/4jug PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jug ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMA_I18A0 HEMA_I18A0]] 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).
+[https://www.uniprot.org/uniprot/HEMA_I18A0 HEMA_I18A0] 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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 20: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Fan, Z]]
+[[Category: Large Structures]]
-[[Category: Gao, F]]
+[[Category: Fan Z]]
-[[Category: Gao, G F]]
+[[Category: Gao F]]
-[[Category: Li, Q]]
+[[Category: Gao GF]]
-[[Category: Qi, J]]
+[[Category: Li Q]]
-[[Category: Shi, Y]]
+[[Category: Qi J]]
-[[Category: Yan, J]]
+[[Category: Shi Y]]
-[[Category: Zhang, W]]
+[[Category: Yan J]]
-[[Category: Membrane fusion]]
+[[Category: Zhang W]]
-[[Category: Viral protein]]
-[[Category: Virus attachment]]