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Publication Abstract from PubMed

Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the alphaalpha hubs, as they share an alphaalpha-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity.

Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alphaalpha-Scaffold for Disorder in Transcriptional Networks.,Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB Structure. 2018 Apr 12. pii: S0969-2126(18)30094-7. doi:, 10.1016/j.str.2018.03.013. PMID:29657132^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.