3mlh: Difference between revisions

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<StructureSection load='3mlh' size='340' side='right'caption='[[3mlh]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
<StructureSection load='3mlh' size='340' side='right'caption='[[3mlh]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3mlh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_a_virus_(a/mexico/4603/2009(h1n1)) Influenza a virus (a/mexico/4603/2009(h1n1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLH FirstGlance]. <br>
<table><tr><td colspan='2'>[[3mlh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Influenza_A_virus_(A/Mexico/4603/2009(H1N1)) Influenza A virus (A/Mexico/4603/2009(H1N1))]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MLH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.09&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=644887 Influenza A virus (A/Mexico/4603/2009(H1N1))])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3mlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlh OCA], [https://pdbe.org/3mlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlh RCSB], [https://www.ebi.ac.uk/pdbsum/3mlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlh 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=3mlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mlh OCA], [https://pdbe.org/3mlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mlh RCSB], [https://www.ebi.ac.uk/pdbsum/3mlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mlh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/C4RSQ3_9INFA C4RSQ3_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.[RuleBase:RU003324][SAAS:SAAS00145386]  
[https://www.uniprot.org/uniprot/C4RSQ3_9INFA C4RSQ3_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.[RuleBase:RU003324][SAAS:SAAS00145386]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aguilar-Yanez, J M]]
[[Category: Aguilar-Yanez JM]]
[[Category: Alvarez, M M]]
[[Category: Alvarez MM]]
[[Category: DuBois, R M]]
[[Category: DuBois RM]]
[[Category: Mendoza-Ochoa, G I]]
[[Category: Mendoza-Ochoa GI]]
[[Category: Russell, C J]]
[[Category: Russell CJ]]
[[Category: Schultz-Cherry, S]]
[[Category: Schultz-Cherry S]]
[[Category: White, S W]]
[[Category: White SW]]
[[Category: Antigen]]
[[Category: Hemagglutinin]]
[[Category: Lectin]]
[[Category: Receptor-binding domain]]
[[Category: Viral protein]]