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Conformational Selection of Dimethylarginine Recognition by the Survival Motor Neuron Tudor Domain
Author(s) -
Supekar Shreyas,
Papageorgiou Anna C.,
Gemmecker Gerd,
Peltzer Raphael,
Johansson Mikael P.,
Tripsianes Konstantinos,
Sattler Michael,
Kaila Ville R. I.
Publication year - 2018
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201708233
Subject(s) - nuclear magnetic resonance spectroscopy , ligand (biochemistry) , molecular recognition , chemistry , asymmetric dimethylarginine , mechanism (biology) , computational biology , biophysics , stereochemistry , biology , biochemistry , receptor , physics , amino acid , arginine , molecule , organic chemistry , quantum mechanics
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–π interactions to achieve ligand recognition.