Study of Protein-Protein Interactions in Septin Assembly: Multiple amphipathic helix domains cooperate in binding to the lipid membrane
Fig 6
Proposed mechanism of septin polymerization on the curved lipid bilayer.
(A) The bound septin facilitates the binding of neighboring septins through salt bridge interactions between their AH domains in anti-parallel, forming septin assemblies. (B) Multiple sequence alignment and sequence logo of the Cdc12 amphipathic helix domain across fungal species. Conserved charged residues implicated in inter-peptide salt bridges are highlighted, including arginine residues in the N-terminal ERIR motif and glutamic acid residues in the LEE motif. These charged residues are instrumental to salt bridge interactions and peptide-peptide contacts.