The viral fusion protein hemagglutinin (HA) is the predominant influenza surface glycoprotein and mediates engagement with and entry into host cells. Influenza A virus HAs are categorised into two broad and immunologically distinct phylogenetic groups. Group 2 HA subtypes include H3, which is found in a large proportion of seasonal influenzas, and H7, which is present in some highly pathogenic avian influenzas. HA is a single-pass, type I transmembrane protein and exists as a trimeric assembly on the surface of the influenza virus. Viral membrane fusion is induced through large, and relatively well characterised, conformational changes in the HA ectodomain. In contrast, very little is known about the architecture of HA’s interaction with the phospholipid bilayer. To date, the only structural information about HA’s transmembrane domain is derived from a group 1, H1 subtype in the prefusion conformation. Here, we present our latest findings pertaining to the structure and function of group 2 HAs, with particular emphasis on their membrane interaction interfaces and how these regions are modulated across HA’s dynamic conformational landscape.