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http://purl.uniprot.org/unirules/MF_04200#construct-template-83http://spinrdf.org/sp#subjecthttp://purl.uniprot.org/unirules/MF_04200#construct-var-4
http://purl.uniprot.org/unirules/MF_04200#construct-template-83http://spinrdf.org/sp#predicatehttp://www.w3.org/2000/01/rdf-schema#comment
http://purl.uniprot.org/unirules/MF_04200#construct-template-83http://spinrdf.org/sp#object"S1 region attaches the virion to the cell membrane by interacting with the host receptor, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes."xsd:string
http://purl.uniprot.org/unirules/MF_04200#constructhttps://hamap.expasy.org/rdf/vocab#addsTriplehttp://purl.uniprot.org/unirules/MF_04200#construct-template-83
http://purl.uniprot.org/unirules/MF_04200#construct-template-list-83http://www.w3.org/1999/02/22-rdf-syntax-ns#firsthttp://purl.uniprot.org/unirules/MF_04200#construct-template-83