4edb: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4edb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Thailand/CU44/2006(H1N1)) Influenza A virus (A/Thailand/CU44/2006(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EDB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EDB FirstGlance]. <br>
-</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=4edb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edb OCA], [https://pdbe.org/4edb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edb RCSB], [https://www.ebi.ac.uk/pdbsum/4edb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edb ProSAT]</span></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]] 2.5&#8491;</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=4edb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4edb OCA], [https://pdbe.org/4edb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4edb RCSB], [https://www.ebi.ac.uk/pdbsum/4edb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4edb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/A7LI25_9INFA A7LI25_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:SAAS001364_004_327643]
+[https://www.uniprot.org/uniprot/A7LI25_9INFA A7LI25_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:SAAS001364_004_327643]
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 == Publication Abstract from PubMed ==