04D623A7ECDB7041A167DBD83372A7B27EDAF99FEAE9A68C30AA70F519BB7B51BA22E99CBB3596E27DC562148B7E902B

S1 region attaches the virion to the cell membrane by interacting with porcine ANPEP/aminopeptidase N, 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 (By similarity).

Source:http://purl.uniprot.org/SHA-384/04D623A7ECDB7041A167DBD83372A7B27EDAF99FEAE9A68C30AA70F519BB7B51BA22E99CBB3596E27DC562148B7E902B

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
rdfs:comment
S1 region attaches the virion to the cell membrane by interacting with porcine ANPEP/aminopeptidase N, 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 (By similarity).