7BOC

Crystal structure of the PRMT5 TIM barrel domain in complex with RioK1 peptide

7BOC の概要

• エントリーDOI: 10.2210/pdb7boc/pdb
• 分子名称: Protein arginine N-methyltransferase 5, peptide (2 entities in total)
• 機能のキーワード: tim barrel, methyltransferase, histones, chromatin-regulator, protein-peptide interaction, transferase
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34873.76

構造登録者

Krzyzanowski, A.,t Hart, P.,Waldmann, H.,Gasper, R. (登録日: 2021-01-25, 公開日: 2021-09-15, 最終更新日: 2024-01-31)

主引用文献

Krzyzanowski, A.,Gasper, R.,Adihou, H.,t Hart, P.,Waldmann, H.
Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5-MEP50 Complex.
Chembiochem, 22:1908-1914, 2021

PubMed Abstract: The PRMT5-MEP50 methyltransferase complex plays a key role in various cancers and is regulated by different protein-protein interactions. Several proteins have been reported to act as adaptor proteins that recruit substrate proteins to the active site of PRMT5 for the methylation of arginine residues. To define the interaction between these adaptor proteins and PRMT5, we employed peptide truncation and mutation studies and prepared truncated protein constructs. We report the characterisation of the interface between the TIM barrel of PRMT5 and the adaptor proteins pICln, RioK1 and COPR5, and identify the consensus amino acid sequence GQF[D/E]DA[E/D] involved in binding. Protein crystallography revealed that the RioK1 derived peptide interacts with a novel PPI site.

PubMed: 33624332
DOI: 10.1002/cbic.202100079

実験手法

X-RAY DIFFRACTION (2.55 Å)