4uo0: Difference between revisions

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 ==Structure of the A_Equine_Richmond_07 H3 haemagglutinin==
-<StructureSection load='4uo0' size='340' side='right' caption='[[4uo0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='4uo0' size='340' side='right'caption='[[4uo0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4uo0]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UO0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4uo0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/equine/Richmond/1/2007(H3N8)) Influenza A virus (A/equine/Richmond/1/2007(H3N8))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UO0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UO0 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4unw|4unw]], [[4unx|4unx]], [[4uny|4uny]], [[4unz|4unz]], [[4uo1|4uo1]], [[4uo2|4uo2]], [[4uo3|4uo3]], [[4uo4|4uo4]], [[4uo5|4uo5]], [[4uo6|4uo6]], [[4uo7|4uo7]], [[4uo8|4uo8]], [[4uo9|4uo9]], [[4uoa|4uoa]]</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=4uo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uo0 OCA], [http://pdbe.org/4uo0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uo0 RCSB], [http://www.ebi.ac.uk/pdbsum/4uo0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uo0 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=4uo0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uo0 OCA], [https://pdbe.org/4uo0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uo0 RCSB], [https://www.ebi.ac.uk/pdbsum/4uo0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uo0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C3TUR9_9INFA C3TUR9_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 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).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]
+[https://www.uniprot.org/uniprot/C3TUR9_9INFA C3TUR9_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 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).[RuleBase:RU003324][SAAS:SAAS008980_004_327643]
 <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: Collins, P J]]
+[[Category: Large Structures]]
-[[Category: Gamblin, S J]]
+[[Category: Collins PJ]]
-[[Category: Haire, L F]]
+[[Category: Gamblin SJ]]
-[[Category: Martin, S R]]
+[[Category: Haire LF]]
-[[Category: Ogrodowicz, R W]]
+[[Category: Martin SR]]
-[[Category: Skehel, J J]]
+[[Category: Ogrodowicz RW]]
-[[Category: Vachieri, S G]]
+[[Category: Skehel JJ]]
-[[Category: Walker, P A]]
+[[Category: Vachieri SG]]
-[[Category: Xiong, X]]
+[[Category: Walker PA]]
-[[Category: Influenza]]
+[[Category: Xiong X]]
-[[Category: Viral protein]]