v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | The rotavirus outer capsid consists of the coat glycoprotein VP7 and the spike protein VP4. VP4 functions in cell attachment and membrane penetration. VP4 is cleaved by the host's trypsin-like proteases to produce two fragments, VP5 and VP8. VP8 functions as a viral haemagglutinin to bind sialic acid receptors on host cell membranes, while VP5 is a membrane penetration protein [ ]. The haemagglutinin domain has a β-sandwich fold similar to that of the sugar-binding galectins family of proteins [, ]. The receptor-binding specificity of rotaviruses by VP4 may be influenced by the VP7 protein.This entry represents the N-terminal concanavalin-like domain from the VP4 protein of rotavirus. |
| Short Name | VP4_concanavalin-like |