Fig. 8: Model for the oligomeric state and conformation of TEX12 wild-type and Ctip mutants.
From: Coiled-coil structure of meiosis protein TEX12 and conformational regulation by its C-terminal tip
a–d The oligomeric state and conformation of TEX12 wild-type and Ctip mutants in solution can be explained by their conserved dimer, tetramer and Ctip interfaces. a TEX12 FFV dimers associate into tetramers that are stabilised by Ctip interfaces at either end of the molecule, accounting for the sole presence of extended tetramers in solution. b TEX12 ΔCtip and c TEX12 LFIL dimers associate into tetramers that remain unstable owing to their deleted and disrupted Ctip interfaces, accounting for the concentration-dependent dissociation of tetramers into mixtures of tetramers and dimers in solution. d Wild-type TEX12 dimers fold back on themselves by adopting helix–loop–helix structures in which the hinge transitions from α-helical to looped conformations. In this structure, the dimer and tetramer interfaces are formed by only two chains, and are stabilised by a Ctip interface supported by intact F102 and V116 amino-acids, accounting for the sole presence of compact dimers in solutions.
