Both TRFs are separate homodimer proteins, similar to the Myb helix-turn-helix motif with DNA binding folds at the C-terminus. There are highly conserved regions located in the centre with relation to the formation of homodimers. However, they differ in the N-terminus as TERF2 contains a basic motif while TERF1 is acidic so they do not dimerize. There is a 120˚ angular bend in TERF1 when binding to the telomeric site.
