4BWS

Crystal structure of the heterotrimer of PQBP1, U5-15kD and U5-52kD.

4BWS の概要

• エントリーDOI: 10.2210/pdb4bws/pdb
• 関連するPDBエントリー: 4BWQ
• 分子名称: THIOREDOXIN-LIKE PROTEIN 4A, POLYGLUTAMINE-BINDING PROTEIN 1, CD2 ANTIGEN CYTOPLASMIC TAIL-BINDING PROTEIN 2, ... (4 entities in total)
• 機能のキーワード: transcription, neurodegenerative disorders
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Nucleus: P83876 O60828; Cytoplasm: O95400
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 58203.60

構造登録者

Mizuguchi, M.,Obita, T.,Serita, T.,Kojima, R.,Morimoto, T.,Nabeshima, Y.,Okazawa, H. (登録日: 2013-07-04, 公開日: 2014-04-30, 最終更新日: 2023-12-20)

主引用文献

Mizuguchi, M.,Obita, T.,Serita, T.,Kojima, R.,Nabeshima, Y.,Okazawa, H.
Mutations in the Pqbp1 Gene Prevent its Interaction with the Spliceosomal Protein U5-15Kd.
Nat.Commun., 5:3822-, 2014

PubMed Abstract: A loss-of-function of polyglutamine tract-binding protein 1 (PQBP1) induced by frameshift mutations is believed to cause X-linked mental retardation. However, the mechanism by which structural changes in PQBP1 lead to mental retardation is unknown. Here we present the crystal structure of a C-terminal fragment of PQBP1 in complex with the spliceosomal protein U5-15 kD. The U5-15 kD hydrophobic groove recognizes a YxxPxxVL motif in PQBP1, and mutations within this motif cause a loss-of-function phenotype of PQBP1 in vitro. The YxxPxxVL motif is absent in all PQBP1 frameshift mutants seen in cases of mental retardation. These results suggest a mechanism by which the loss of the YxxPxxVL motif could lead to the functional defects seen in this type of mental retardation.

PubMed: 24781215
DOI: 10.1038/NCOMMS4822

実験手法

X-RAY DIFFRACTION (2.5 Å)