9iyx
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of HBV surface antigen determined in recombinant spherical subviral particle== | |
| - | + | <StructureSection load='9iyx' size='340' side='right'caption='[[9iyx]], [[Resolution|resolution]] 3.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[9iyx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/HBV_genotype_D3 HBV genotype D3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9IYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9IYX FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=9iyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9iyx OCA], [https://pdbe.org/9iyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9iyx RCSB], [https://www.ebi.ac.uk/pdbsum/9iyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9iyx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/V9P415_HBV V9P415_HBV] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein.[HAMAP-Rule:MF_04075] The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid.[HAMAP-Rule:MF_04075] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: HBV genotype D3]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen L]] | ||
| + | [[Category: He X]] | ||
Current revision
Structure of HBV surface antigen determined in recombinant spherical subviral particle
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