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  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. (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.

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Genre: Journal Article

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 Creators:
Orth, B.1, Author           
Sander, B., Author
Möglich, A., Author
Diederichs, K., Author
Eilers, M., Author
Lorenz, S.1, Author           
Affiliations:
1Research Group Ubiquitin Signaling Specificity, MPI for Biophysical Chemistry, Max Planck Society, ou_3337583              

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Free keywords: MIZ1; POZ domain; dimerization; homodimer; heterodimer; protein-protein interaction; transcription; HUWE1; X-ray crystallography fluorescence polarization
 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.

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Language(s): eng - English
 Dates: 2021-06-28
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.str.2021.06.005 Get
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Title: Structure
Source Genre: Journal
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Pages: - Volume / Issue: 29 (11) Sequence Number: - Start / End Page: 1230 - 1240 Identifier: -