5OAP
Solution NMR structure of DREB2A(255-272) bound to RCD1-RST
Summary for 5OAP
| Entry DOI | 10.2210/pdb5oap/pdb |
| NMR Information | BMRB: 34152 |
| Descriptor | DREB2A (1 entity in total) |
| Functional Keywords | plant protein, transcription factor, folding upon binding, idp, transcription |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 2057.13 |
| Authors | Bugge, K.,Staby, L.,Skriver, K.,Kragelund, B.B. (deposition date: 2017-06-23, release date: 2018-04-18, Last modification date: 2024-06-19) |
| Primary citation | Bugge, K.,Staby, L.,Kemplen, K.R.,O'Shea, C.,Bendsen, S.K.,Jensen, M.K.,Olsen, J.G.,Skriver, K.,Kragelund, B.B. Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alpha alpha-Scaffold for Disorder in Transcriptional Networks. Structure, 26:734-746.e7, 2018 Cited by PubMed Abstract: 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 αα hubs, as they share an αα-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. PubMed: 29657132DOI: 10.1016/j.str.2018.03.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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