9r6r

Local refinement of the N-terminal domain (NTD) from the Porcine hemagglutinating encephalomyelitis virus (PHEV) Spike in the open conformation bound to 9-O-Ac-Sia

spinqualitylabelsall models 9r6r, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9r6r is a 1 chain structure with sequence from Porcine hemagglutinating encephalomyelitis virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: 5N6, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2QKN3_9BETC Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099] Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three 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) 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.[HAMAP-Rule:MF_04099]

Proteopedia Page Contributors and Editors (what is this?)

OCA