Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain

Warning

This publication doesn't include Faculty of Medicine. It includes Central European Institute of Technology. Official publication website can be found on muni.cz.

Authors	SUPEKAR S. PAPAGEORGIOU Anna GEMMECKER G. PELTZER R. JOHANSSON M.P. TRIPSIANES Konstantinos SATTLER M. KAILA V.R.I.
Year of publication	2018
Type	Article in Periodical
Magazine / Source	Angewandte Chemie International Edition
MU Faculty or unit	Central European Institute of Technology
Citation
Doi	http://dx.doi.org/10.1002/anie.201708233
Keywords	arginine rotation; cation-p interactions; dynamic NMR; QM/MM; quantum chemistry
Description	Tudor domains bind to dimethylarginine (DMA) residues, which are post-translational modifications that play a central role in gene regulation in eukaryotic cells. NMR spectroscopy and quantum calculations are combined to demonstrate that DMA recognition by Tudor domains involves conformational selection. The binding mechanism is confirmed by a mutation in the aromatic cage that perturbs the native recognition mode of the ligand. General mechanistic principles are delineated from the combined results, indicating that Tudor domains utilize cation-p interactions to achieve ligand recognition.
Related projects:	Molekulární stavba protein-DNA komplexů zapojených v opravě nukleotidových sestřihů CEITEC 2020