4bh0: Difference between revisions

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 <StructureSection load='4bh0' size='340' side='right'caption='[[4bh0]], [[Resolution|resolution]] 2.36&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4bh0]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BH0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4bh0]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/turkey/Turkey/1/2005(H5N1)) Influenza A virus (A/turkey/Turkey/1/2005(H5N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BH0 FirstGlance]. <br>
-</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>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</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]] 2.36&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=PRD_900046:6-sialyl-N-acetyllactosamine'>PRD_900046</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bgw|4bgw]], [[4bgx|4bgx]], [[4bgy|4bgy]], [[4bgz|4bgz]], [[4bh1|4bh1]], [[4bh2|4bh2]], [[4bh3|4bh3]], [[4bh4|4bh4]]</div></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=4bh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bh0 OCA], [https://pdbe.org/4bh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bh0 RCSB], [https://www.ebi.ac.uk/pdbsum/4bh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bh0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/Q207Z6_9INFA Q207Z6_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/Q207Z6_9INFA Q207Z6_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 28: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Collins, P J]]
+[[Category: Collins PJ]]
-[[Category: Coombs, P J]]
+[[Category: Coombs PJ]]
-[[Category: Gamblin, S J]]
+[[Category: Gamblin SJ]]
-[[Category: Kawaoka, Y]]
+[[Category: Kawaoka Y]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Locher, K]]
+[[Category: Locher K]]
-[[Category: Martin, S R]]
+[[Category: Martin SR]]
-[[Category: McCauley, J W]]
+[[Category: McCauley JW]]
-[[Category: Skehel, J J]]
+[[Category: Skehel JJ]]
-[[Category: Walker, P A]]
+[[Category: Walker PA]]
-[[Category: Xiao, H]]
+[[Category: Xiao H]]
-[[Category: Xiong, X]]
+[[Category: Xiong X]]
-[[Category: Bird flu]]
-[[Category: N-glycosylation]]
-[[Category: Viral protein]]
-[[Category: Virus receptor]]