A beta bend ribbon can be regarded as an aberrant 310 helix (3/10-helix) that has lost some of its hydrogen bonds.
Type I beta-bend ribbons regularly occur in leucine-rich repeats, in the environments sometimes occupied by helices.
A protein with a stack of these features is the extracellular ligand-binding domain of the Nogo receptor.
[13] Another beta bend ribbon occurs in the GTPase-activating protein for Rho in the active, but not the inactive, form of the enzyme.
[14] Polypeptides consisting of repeats of the dipeptide (α-amino-γ-lactam plus a conventional amino acid) have been shown to adopt a beta bend ribbon conformation.