2BKD

Structure of the N-terminal domain of Fragile X Mental Retardation Protein

2BKD の概要

• エントリーDOI: 10.2210/pdb2bkd/pdb
• 関連するPDBエントリー: 2FMR
• 分子名称: Fragile X messenger ribonucleoprotein 1 (1 entity in total)
• 機能のキーワード: fmrp, protein-protein interaction, mrna transport, nuclear protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus . Isoform 6: Cytoplasm . Isoform 9: Cytoplasm . Isoform 10: Nucleus . Isoform 11: Nucleus : Q06787
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15618.60

構造登録者

Ramos, A.,Hollingworth, D.,Adinolfi, S.,Castets, M.,Kelly, G.,Frenkiel, T.A.,Bardoni, B.,Pastore, A. (登録日: 2005-02-15, 公開日: 2006-01-18, 最終更新日: 2024-11-06)

主引用文献

Ramos, A.,Hollingworth, D.,Adinolfi, S.,Castets, M.,Kelly, G.,Frenkiel, T.A.,Bardoni, B.,Pastore, A.
The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction.
Structure, 14:21-31, 2006

PubMed Abstract: FMRP, whose lack of expression causes the X-linked fragile X syndrome, is a modular RNA binding protein thought to be involved in posttranslational regulation. We have solved the structure in solution of the N-terminal domain of FMRP (NDF), a functionally important region involved in multiple interactions. The structure consists of a composite fold comprising two repeats of a Tudor motif followed by a short alpha helix. The interactions between the three structural elements are essential for the stability of the NDF fold. Although structurally similar, the two repeats have different dynamic and functional properties. The second, more flexible repeat is responsible for interacting both with methylated lysine and with 82-FIP, one of the FMRP nuclear partners. NDF contains a 3D nucleolar localization signal, since destabilization of its fold leads to altered nucleolar localization of FMRP. We suggest that the NDF composite fold determines an allosteric mechanism that regulates the FMRP functions.

PubMed: 16407062
DOI: 10.1016/j.str.2005.09.018

実験手法

SOLUTION NMR