5OAO

Solution structure of the complexed RCD1-RST

5OAO の概要

• エントリーDOI: 10.2210/pdb5oao/pdb
• NMR情報: BMRB: 34151
• 分子名称: RST domain from the Radical-Induced Cell Death1 (1 entity in total)
• 機能のキーワード: alpha-alpha hairpin, hub, l-glove, transcription factor binding, protein binding
• 由来する生物種: Arabidopsis thaliana (Mouse-ear cress)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8455.85

構造登録者

Bugge, K.,Staby, L.,Skriver, K.,Kragelund, B.B. (登録日: 2017-06-23, 公開日: 2018-04-18, 最終更新日: 2024-06-19)

主引用文献

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

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: 29657132
DOI: 10.1016/j.str.2018.03.013

実験手法

SOLUTION NMR