3HFH

Crystal structure of tandem FF domains

3HFH の概要

• エントリーDOI: 10.2210/pdb3hfh/pdb
• 分子名称: Transcription elongation regulator 1 (2 entities in total)
• 機能のキーワード: helix bundle, activator, alternative splicing, coiled coil, nucleus, phosphoprotein, repressor, transcription, transcription regulation, transcription regulator
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : O14776
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47661.35

構造登録者

Lu, M.,Yang, J.,Ren, Z.,Subir, S.,Bedford, M.T.,Jacobson, R.H.,McMurray, J.S.,Chen, X. (登録日: 2009-05-11, 公開日: 2009-08-18, 最終更新日: 2025-03-26)

主引用文献

Lu, M.,Yang, J.,Ren, Z.,Sabui, S.,Espejo, A.,Bedford, M.T.,Jacobson, R.H.,Jeruzalmi, D.,McMurray, J.S.,Chen, X.
Crystal Structure of the Three Tandem FF Domains of the Transcription Elongation Regulator CA150.
J.Mol.Biol., 393:397-408, 2009

PubMed Abstract: FF domains are small protein-protein interaction modules that have two flanking conserved phenylalanine residues. They are present in proteins involved in transcription, RNA splicing, and signal transduction, and often exist in tandem arrays. Although several individual FF domain structures have been determined by NMR, the tandem nature of most FF domains has not been revealed. Here we report the 2.7-A-resolution crystal structure of the first three FF domains of the human transcription elongation factor CA150. Each FF domain is composed of three alpha-helices and a 3(10) helix between alpha-helix 2 and alpha-helix 3. The most striking feature of the structure is that an FF domain is connected to the next by an alpha-helix that continues from helix 3 to helix 1 of the next. The consequent elongated arrangement allows exposure of many charged residues within the region that can be engaged in interaction with other molecules. Binding studies using a peptide ligand suggest that a specific conformation of the FF domains might be required to achieve higher-affinity binding. Additionally, we explore potential DNA binding of the FF construct used in this study. Overall, we provide the first crystal structure of an FF domain and insights into the tandem nature of the FF domains and suggest that, in addition to protein binding, FF domains might be involved in DNA binding.

PubMed: 19660470
DOI: 10.1016/j.jmb.2009.07.086

実験手法

X-RAY DIFFRACTION (2.703 Å)