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

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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.
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