Abstract 2453 Tuning the conformational ensembles of IDPs through intramolecular and intermolecular interactions
The intrinsically disordered protein CITED2 is essential in regulating the transcriptional response to oxygen deficiency and other key cellular processes that are important for human health and are often disrupted in disease. CITED2 is a fully disordered protein with interaction motifs positioned throughout the protein sequence that engage a diverse set of molecular partners through dynamic, multivalent interactions. While the interactions of the C-terminal transcriptional activation domain of CITED2 are well-characterized, little is known about the functional roles of the CITED2 N-terminus and its potential impacts on interactions of CITED2 with other transcriptional regulators.
Authors
- Rebecca B. Berlow (ORCID: https://orcid.org/0000-0003-1934-0139)
- Garrett Chappell (ORCID: https://orcid.org/0000-0002-0078-1498)
- J A Simmons (ORCID: https://orcid.org/0009-0003-6281-0391)
- To Uyen
- Morgan Opp
- Elise Liebow
Institutions
- University of North Carolina at Chapel Hill (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109999
- Primary Topic
- Chemical Synthesis and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00