Structure of coronavirus hemagglutinin-esterase in complex with 4,9-O-diacetyl sialic acidStructure of coronavirus hemagglutinin-esterase in complex with 4,9-O-diacetyl sialic acid
Structural highlights
3cl5 is a 1 chain structure with sequence from Bovine coronavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
HEMA_CVBM Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-9-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptible cells. This receptor-destroying activity is important for virus release as it probably helps preventing self-aggregation and ensures the efficient spread of the progeny virus from cell to cell. May serve as a secondary viral attachment protein for initiating infection, the spike protein being the major one. Seems to be a 'luxury' protein that is not absolutely necessary for virus infection in culture. However, its presence in the virus may alter its pathogenicity. May become a target for both the humoral and the cellular branches of the immune system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
