7AZW

Crystal structure of the MIZ1-BTB-domain

Summary for 7AZW

• Entry DOI: 10.2210/pdb7azw/pdb
• Descriptor: Zinc finger and BTB domain-containing protein 17 isoform X1, GLYCEROL (3 entities in total)
• Functional Keywords: btb-domain, transcription factor, dimer, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 26654.65

Authors

Orth, B.,Sander, B.,Diederichs, K.,Lorenz, S. (deposition date: 2020-11-17, release date: 2021-06-23, Last modification date: 2024-01-31)

Primary citation

Orth, B.,Sander, B.,Moglich, A.,Diederichs, K.,Eilers, M.,Lorenz, S.
Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1.
Structure, 29:1230-1240.e5, 2021

PubMed 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.

PubMed: 34186024
DOI: 10.1016/j.str.2021.06.005

Experimental method

X-RAY DIFFRACTION (2.1 Å)