Identification of an atypical interaction site in the BTB domain of the 
MYC-interacting zinc-finger protein 1

Orth, B.; Sander, B.; Möglich, A.; Diederichs, K.; Eilers, M.; Lorenz, S.

doi:10.1016/j.str.2021.06.005 Get

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Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1

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Orth, B.
Research Group Ubiquitin Signaling Specificity, MPI for Biophysical Chemistry, Max Planck Society;

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Lorenz, S.
Research Group Ubiquitin Signaling Specificity, MPI for Biophysical Chemistry, Max Planck Society;

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Citation

Orth, B., Sander, B., Möglich, A., Diederichs, K., Eilers, M., & Lorenz, S. (2021). Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1. Structure, 29(11), 1230-1240. doi:10.1016/j.str.2021.06.005 Get.

Cite as: https://hdl.handle.net/21.11116/0000-0009-1164-3

Abstract

The repurposing of structurally conserved protein domains in different functional contexts is thought to be a driving force in the evolution of complex protein interaction networks. The BTB/POZ domain is such a versatile binding module that occurs over 200 times in the human proteome with diverse protein-specific adaptations. In BTB-zinc-finger transcription factors, the BTB domain drives homo- and heterodimerization as well as interactions with non-BTB-domain-containing proteins. Which mechanisms encode specificity in these interactions at a structural level is incompletely understood. Here, we uncover an atypical peptide-binding site in the BTB domain of the MYC-interacting zinc-finger protein 1 (MIZ1) that arises from local flexibility of the core BTB fold and may provide a target site for MIZ1-directed therapeutic approaches. Intriguingly, the identified binding mode requires the BTB domain to be in a homodimeric state, thus holding opportunities for functional discrimination between homo- and heterodimers of MIZ1 in the cell.