Ontology highlight
ABSTRACT:
SUBMITTER: Sabirov M
PROVIDER: S-EPMC8618245 | biostudies-literature | 2021 Nov
REPOSITORIES: biostudies-literature
Sabirov Marat M Popovich Anastasia A Boyko Konstantin K Nikolaeva Alena A Kyrchanova Olga O Maksimenko Oksana O Popov Vladimir V Georgiev Pavel P Bonchuk Artem A
International journal of molecular sciences 20211117 22
Most of the known Drosophila architectural proteins interact with an important cofactor, CP190, that contains three domains (BTB, M, and D) that are involved in protein-protein interactions. The highly conserved N-terminal CP190 BTB domain forms a stable homodimer that interacts with unstructured regions in the three best-characterized architectural proteins: dCTCF, Su(Hw), and Pita. Here, we identified two new CP190 partners, CG4730 and CG31365, that interact with the BTB domain. The CP190 BTB ...[more]