Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers

Higher‐order structure formation using refined monomer structures of lipid raft markers, Stomatin, Prohibitin, Flotillin, and HflK/C‐related proteins

“…Recently, we revealed the difference in the oligomerization state of stomatin orthologs as the core domain of mouse stomatin was reported to form a dimer [ 4 ]; however, PhSto CD is a trimer. The key residues of PH1511, 56–62 and 162–168, were suggested to determine whether SPFH domains form a dimer or trimer structure [ 5 ]. As an intact 3D structure of the PH1511 monomer was lacking, it was difficult to predict a higher‐order structure consisting of homo‐oligomers.…”