Atomic structures and deletion mutant reveal different capsid-binding patterns and functional significance of tegument protein pp150 in murine and human cytomegaloviruses with implications for therapeutic development
Fig 5
Structure of triplex and functional significance of Tri1 N-anchor.
(A) Distribution of triplexes Ta, Tb, Tc, Td, and Te among penton and three types of hexons (C, E, and P). (B) Enlarged view of a triplex Td with three adjacent hexon MCP subunits labeled (C1, E5, and P3). (C-D) Details of the structures of triplex Td (C) and Tri1 (D). (E) Bottom view of (B) showing that triplex Td anchors to the capsid floor by the “V”-shaped Tri1 N-anchor. (F) Triplex Td viewed from inside of the capsid showing similar clamp and trunk domains, albeit rotated about 120° relative to each other. (G) Pipe-and-plank representations of Tri2 dimer in side (left panel) and top (right panel) views showing the helix bundle formed from Tri2A and Tri2B’s embracing arm domains. (H) Superposition of Tri2A and Tri2B showing nearly identical clamp and trunk domains, but different embracing arms.