Structural analysis of the PATZ1 BTB domain homodimer.pdf (3.19 MB)
Structural analysis of the PATZ1 BTB domain homodimer
journal contribution
posted on 2023-06-09, 21:40 authored by Sofia Piepoli, Aaron Oliver Alt, Canan Atilgan, Erika ManciniErika Mancini, Batu ErmanPATZ1 is a ubiquitously expressed transcriptional repressor belonging to the ZBTB family that is functionally expressed in T lymphocytes. PATZ1 targets the CD8 gene in lymphocyte development and interacts with the p53 protein to control genes that are important in proliferation and in the DNA-damage response. PATZ1 exerts its activity through an N-terminal BTB domain that mediates dimerization and co-repressor interactions and a C-terminal zinc-finger motif-containing domain that mediates DNA binding. Here, the crystal structures of the murine and zebrafish PATZ1 BTB domains are reported at 2.3 and 1.8 Å resolution, respectively. The structures revealed that the PATZ1 BTB domain forms a stable homodimer with a lateral surface groove, as in other ZBTB structures. Analysis of the lateral groove revealed a large acidic patch in this region, which contrasts with the previously resolved basic co-repressor binding interface of BCL6. A large 30-amino-acid glycine- and alanine-rich central loop, which is unique to mammalian PATZ1 amongst all ZBTB proteins, could not be resolved, probably owing to its flexibility. Molecular-dynamics simulations suggest a contribution of this loop to modulation of the mammalian BTB dimerization interface.
History
Publication status
- Published
File Version
- Published version
Journal
Acta Crystallographica Section D: Structural BiologyISSN
2059-7983Publisher
International Union of CrystallographyExternal DOI
Volume
76Page range
581-593Event location
United StatesDepartment affiliated with
- Biochemistry Publications
Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2020-09-25First Open Access (FOA) Date
2020-09-25First Compliant Deposit (FCD) Date
2020-09-25Usage metrics
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