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Supekar, S.* ; Papageorgiou, A.C.* ; Gemmecker, G. ; Peltzer, R.* ; Johansson, M.P.* ; Tripsianes, K.* ; Sattler, M. ; Kaila, V.R.I.*

Conformational selection of dimethylarginine recognition by the survival motor neuron tudor domain.

Angew. Chem.-Int. Edit. 57, 486-490 (2018)
Verlagsversion DOI
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Arginine Rotation ; Cation–π Interactions ; Dynamic Nmr ; Qm/mm ; Quantum Chemistry; Chemical-vapor-deposition; Ammonia Borane; Thin-films; Nitro/nitrile Compounds; Nanostructure Arrays; Nanoparticle Arrays; Gold Nanoparticles; Efficient Catalyst; Graphene Oxide; Hydrogenation
ISSN (print) / ISBN 1433-7851
e-ISSN 1521-3773
Quellenangaben Band: 57, Heft: 2, Seiten: 486-490 Artikelnummer: , Supplement: ,
Verlag Wiley
Verlagsort Weinheim
Begutachtungsstatus Peer reviewed