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http://purl.uniprot.org/unirules/MF_04075#construct-template-98http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_04075#construct-var-7
http://purl.uniprot.org/unirules/MF_04075#construct-template-98http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_04075#construct-template-98http://spinrdf.org/sp#object"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."xsd:string
http://purl.uniprot.org/unirules/MF_04075#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_04075#construct-template-98
http://purl.uniprot.org/unirules/MF_04075#construct-template-list-98http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_04075#construct-template-98