FEATURES

FAMILY

DESCRIPTION

Also known as CAPSH_ADE05, L3. Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. Homotrimer. Interacts with the capsid vertex protein; this interaction binds the peripentonal hexons to the neighboring penton base. Interacts with the hexon-linking protein; this interaction tethers the hexons surrounding the penton to those situated in the central plate of the facet. Interacts with the hexon-interlacing protein; this interaction lashes the hexons together. Interacts with host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in intracellular microtubule-dependent transport of incoming viral capsid. Interacts with the shutoff protein; this interaction allows folding and formation of hexons trimers. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly. Interacts with host NUP214 (via N-terminus); this interaction might be essential for the release of the virus genome to the nucleus (PubMed:25410864).

EXTERNAL LINKS

L3

Structural Ligandability

Domains Chains

Distribution