7BOC

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

Summary for 7BOC

• Entry DOI: 10.2210/pdb7boc/pdb
• Descriptor: Protein arginine N-methyltransferase 5, peptide (2 entities in total)
• Functional Keywords: tim barrel, methyltransferase, histones, chromatin-regulator, protein-peptide interaction, transferase
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 34873.76

Authors

Krzyzanowski, A.,t Hart, P.,Waldmann, H.,Gasper, R. (deposition date: 2021-01-25, release date: 2021-09-15, Last modification date: 2024-01-31)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.55 Å)