4fqv: Difference between revisions

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 ==Crystal structure of broadly neutralizing antibody CR9114 bound to H7 influenza hemagglutinin==
-<StructureSection load='4fqv' size='340' side='right' caption='[[4fqv]], [[Resolution|resolution]] 5.75&Aring;' scene=''>
+<StructureSection load='4fqv' size='340' side='right'caption='[[4fqv]], [[Resolution|resolution]] 5.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4fqv]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Influenza_a_virus_(a/netherlands/219/03(h7n7)) Influenza a virus (a/netherlands/219/03(h7n7))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FQV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4fqv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Netherlands/219/2003(H7N7)) Influenza A virus (A/Netherlands/219/2003(H7N7))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FQV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FQV FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fnk|4fnk]], [[4fqh|4fqh]], [[4fqi|4fqi]], [[4fqj|4fqj]], [[4fqk|4fqk]], [[4fql|4fql]], [[4fqm|4fqm]], [[4fqy|4fqy]]</td></tr>
+</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=4fqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqv OCA], [https://pdbe.org/4fqv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fqv RCSB], [https://www.ebi.ac.uk/pdbsum/4fqv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqv ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=680693 Influenza A virus (A/Netherlands/219/03(H7N7))])</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=4fqv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fqv OCA], [http://pdbe.org/4fqv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fqv RCSB], [http://www.ebi.ac.uk/pdbsum/4fqv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fqv ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q6VMK1_9INFA Q6VMK1_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:SAAS013829_004_327643]
+[https://www.uniprot.org/uniprot/Q6VMK1_9INFA Q6VMK1_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:SAAS013829_004_327643]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 19: @@
 ==See Also==
-*[[Hemagglutinin|Hemagglutinin]]
+*[[Antibody 3D structures|Antibody 3D structures]]
+*[[Hemagglutinin 3D structures|Hemagglutinin 3D structures]]
+*[[3D structures of human antibody|3D structures of human antibody]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Dreyfus, C]]
+[[Category: Large Structures]]
-[[Category: Ekiert, D C]]
+[[Category: Dreyfus C]]
-[[Category: Wilson, I A]]
+[[Category: Ekiert DC]]
-[[Category: Immune recognition]]
+[[Category: Wilson IA]]
-[[Category: Immunoglobulin]]
-[[Category: Viral fusion protein]]
-[[Category: Viral protein-immune system complex]]
-[[Category: Virus attachment and entry]]