Hexon coat proteins are synthesised during late infection and form homo-trimers.

The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX.

[1] The hexon coat protein is a duplication consisting of two domains with a similar fold packed together like the nucleoplasmin subunits.

Hexon directly recruits the cellular motor protein dynein in a pH-dependent manner.

[3] The dynein-regulatory protein, dynactin, was found to play a clear role in regulating the dynein-adenovirus complex transport to the nucleus.