4we5: Difference between revisions

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 ==The crystal structure of hemagglutinin from A/Port Chalmers/1/1973 influenza virus==
-<StructureSection load='4we5' size='340' side='right' caption='[[4we5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+<StructureSection load='4we5' size='340' side='right'caption='[[4we5]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4we5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WE5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4we5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Port_Chalmers/1/1973(H3N2)) Influenza A virus (A/Port Chalmers/1/1973(H3N2))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WE5 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4we4|4we4]], [[4we6|4we6]], [[4we7|4we7]], [[4we8|4we8]], [[4we9|4we9]], [[4wea|4wea]]</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='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=4we5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we5 OCA], [http://pdbe.org/4we5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4we5 RCSB], [http://www.ebi.ac.uk/pdbsum/4we5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4we5 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=4we5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4we5 OCA], [https://pdbe.org/4we5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4we5 RCSB], [https://www.ebi.ac.uk/pdbsum/4we5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4we5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HEMA_I73A5 HEMA_I73A5]] 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_I73A5 HEMA_I73A5] 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 21: / Line 21: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Carney, P J]]
+[[Category: Large Structures]]
-[[Category: Chang, J C]]
+[[Category: Carney PJ]]
-[[Category: Guo, Z]]
+[[Category: Chang JC]]
-[[Category: Stevens, J]]
+[[Category: Guo Z]]
-[[Category: Villanueva, J M]]
+[[Category: Stevens J]]
-[[Category: Yang, H]]
+[[Category: Villanueva JM]]
-[[Category: H3n2]]
+[[Category: Yang H]]
-[[Category: Hemagglutinin]]
-[[Category: Influenza virus]]