2KIS

Solution structure of CA150 FF1 domain and FF1-FF2 interdomain linker

2KIS の概要

• エントリーDOI: 10.2210/pdb2kis/pdb
• NMR情報: BMRB: 16293
• 分子名称: Transcription elongation regulator 1 (1 entity in total)
• 機能のキーワード: ff domain, extended helix, interdomain helix, linker peptide, interdomain dynamics, activator, alternative splicing, coiled coil, nucleus, phosphoprotein, repressor, transcription, transcription regulation, transcription regulator
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8577.96

構造登録者

Murphy, J.M.,Hansen, D.,Wiesner, S.,Muhandiram, D.,Borg, M.,Smith, M.J.,Sicheri, F.,Kay, L.E.,Forman-Kay, J.D.,Pawson, T. (登録日: 2009-05-08, 公開日: 2009-09-08, 最終更新日: 2024-05-08)

主引用文献

Murphy, J.M.,Hansen, D.F.,Wiesner, S.,Muhandiram, D.R.,Borg, M.,Smith, M.J.,Sicheri, F.,Kay, L.E.,Forman-Kay, J.D.,Pawson, T.
Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.
J.Mol.Biol., 393:409-424, 2009

PubMed Abstract: FF domains are poorly understood protein interaction modules that are present within eukaryotic transcription factors, such as CA150 (TCERG-1). The CA150 FF domains have been shown to mediate interactions with the phosphorylated C-terminal domain of RNA polymerase II (phosphoCTD) and a multitude of transcription factors and RNA processing proteins, and may therefore have a central role in organizing transcription. FF domains occur in tandem arrays of up to six domains, although it is not known whether they adopt higher-order structures. We have used the CA150 FF1+FF2 domains as a model system to examine whether tandem FF domains form higher-order structures in solution using NMR spectroscopy. In the solution structure of FF1 fused to the linker that joins FF1 to FF2, we observed that the highly conserved linker peptide is ordered and forms a helical extension of helix alpha3, suggesting that the interdomain linker might have a role in orientating FF1 relative to FF2. However, examination of the FF1+FF2 domains using relaxation NMR experiments revealed that although these domains are not rigidly orientated relative to one another, they do not tumble independently. Thus, the FF1+FF2 structure conforms to a dumbbell-shape in solution, where the helical interdomain linker maintains distance between the two dynamic FF domains without cementing their relative orientations. This model for FF domain organization within tandem arrays suggests a general mechanism by which individual FF domains can manoeuvre to achieve optimal recognition of flexible binding partners, such as the intrinsically-disordered phosphoCTD.

PubMed: 19715701
DOI: 10.1016/j.jmb.2009.08.049

実験手法

SOLUTION NMR