6chx: Difference between revisions

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 ==High Resolution Crystal Structure of the Hemagglutinin H1 Head Domain of Influenza A virus Solomon Islands==
-<StructureSection load='6chx' size='340' side='right' caption='[[6chx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+<StructureSection load='6chx' size='340' side='right'caption='[[6chx]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6chx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CHX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6chx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Juliaca/FLU3969/2006(H1N1)) Influenza A virus (A/Juliaca/FLU3969/2006(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CHX FirstGlance]. <br>
-</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=6chx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chx OCA], [http://pdbe.org/6chx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6chx RCSB], [http://www.ebi.ac.uk/pdbsum/6chx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6chx 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]] 1.4&#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=6chx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chx OCA], [https://pdbe.org/6chx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6chx RCSB], [https://www.ebi.ac.uk/pdbsum/6chx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6chx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/D1MNG6_9INFA D1MNG6_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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS01039674]  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.[RuleBase:RU003324]
+[https://www.uniprot.org/uniprot/D1MNG6_9INFA D1MNG6_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 either through clathrin-dependent endocytosis or through 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.[SAAS:SAAS01039674]  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.[RuleBase:RU003324]
+==See Also==
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Crowe, J E]]
+[[Category: Large Structures]]
-[[Category: Dong, J]]
+[[Category: Crowe JE]]
-[[Category: Sevy, A M]]
+[[Category: Dong J]]
-[[Category: Hemagglutinin]]
+[[Category: Sevy AM]]
-[[Category: Influenza a virus]]
-[[Category: Solomon island]]
-[[Category: Viral protein]]