True Arrestins and Arrestin-Fold Proteins: A Structure-Based Appraisal - Progress in Molecular Biology and Translational Science - page 45

Members of the arrestin clan described here share a stable tertiary topol-
ogy essentially made of b -strands. All of them are involved in various intra-
cellular trafficking steps and can thus be considered as relatives. However, no
transversal functional unity emerges from their role in trafficking. In the
arrestin clan, even the closest members are, at most, first cousins, clearly
not twins.
Note added in proof: The structure of the N-terminal domain of
human TXNIP has now been determined [Polekhina, G., Ascher, B. D.,
Kok, S. F., Beckham, S., Wilce, M. and Waltham, M. (2013) Structure
of the N-terminal domain of human thioredoxin-interacting protein. Acta
Cryst. D69, 333-344]. TXNIP adopts an arrestin fold as predicted.

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