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==Crystal structure of Glycoprotein C from Puumala virus in the post-fusion conformation (pH 8.0)==
==Crystal structure of Glycoprotein C from Puumala virus in the post-fusion conformation (pH 8.0)==
<StructureSection load='5j9h' size='340' side='right' caption='[[5j9h]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='5j9h' size='340' side='right'caption='[[5j9h]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5j9h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J9H FirstGlance]. <br>
<table><tr><td colspan='2'>[[5j9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Puumala_virus_p360 Puumala virus p360]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J9H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5j81|5j81]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=5j9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9h OCA], [http://pdbe.org/5j9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j9h RCSB], [http://www.ebi.ac.uk/pdbsum/5j9h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9h 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=5j9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j9h OCA], [https://pdbe.org/5j9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j9h RCSB], [https://www.ebi.ac.uk/pdbsum/5j9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j9h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GP_PUUMP GP_PUUMP]] Glycoprotein N and Glycoprotein C interact with each other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promote fusion of viral membrane with host endosomal membrane after endocytosis of the virion. Glycoprotein N contains an ITAM motif which is likely to dysregulate normal immune and endothelial cell responses and contribute to virus pathogenesis (By similarity).  
[https://www.uniprot.org/uniprot/GP_PUUMP GP_PUUMP] Glycoprotein N and Glycoprotein C interact with each other and are present at the surface of the virion. They are able to attach the virion to host cell receptors. This attachment induces virion internalization predominantly through clathrin-dependent endocytosis. Also promote fusion of viral membrane with host endosomal membrane after endocytosis of the virion. Glycoprotein N contains an ITAM motif which is likely to dysregulate normal immune and endothelial cell responses and contribute to virus pathogenesis (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dessau, M]]
[[Category: Large Structures]]
[[Category: Willensky, S]]
[[Category: Puumala virus p360]]
[[Category: Conformational change]]
[[Category: Dessau M]]
[[Category: Enveloped viruse]]
[[Category: Willensky S]]
[[Category: Hantavirus]]
[[Category: Membrane fusion]]
[[Category: Viral protein]]
[[Category: Virus entry]]