Premium
Front Cover: Biochemical Investigation of the Interaction of pICln, RioK1 and COPR5 with the PRMT5–MEP50 Complex (ChemBioChem 11/2021)
Author(s) -
Krzyzanowski Adrian,
Gasper Raphael,
Adihou Hélène,
Hart Peter 't,
Waldmann Herbert
Publication year - 2021
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202100205
Subject(s) - protein arginine methyltransferase 5 , peptide , signal transducing adaptor protein , alanine , chemistry , binding site , biology , computational biology , microbiology and biotechnology , biochemistry , receptor , amino acid , dna , methylation , methyltransferase
Aligning the adaptor protein sequences : The image shows all sequences derived from PRMT5 adaptor proteins RioK1, pICln and COPR5, that were tested. The consensus sequence GQF[D/E]DA[E/D] was identified, synthesized, and found to bind potently to PRMT5, highlighted as white sequence parts at the highest affinity binding peptides. White alanines represent the sequences, where the mutation to alanine reduced binding between peptide and PRMT5 the most. Protein truncation and the crystal structure of PRMT5 in complex with a RioK1 derived peptide confirmed the binding and illuminated a novel protein–protein interaction site on the TIM‐barrel domain. More information can be found in the Communication by P. ′t Hart, H. Waldmann et al.