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Open Access Green as soon as Postprint is submitted to ZB.
Conformational selection of dimethylarginine recognition by the survival motor neuron tudor domain.
Angew. Chem.-Int. Edit. 57, 486-490 (2018)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
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
Volume: 57,
Issue: 2,
Pages: 486-490
Publisher
Wiley
Publishing Place
Weinheim
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Structural Biology (STB)