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Biomol NMR Assign ; 13(2): 281-286, 2019 10.
Article in English | MEDLINE | ID: mdl-31030336

ABSTRACT

Ligand binding RNAs such as artificially created RNA-aptamers are structurally highly diverse. Therefore, they represent important model systems for investigating RNA-folding, RNA-dynamics and the molecular recognition of chemically very different ligands, ranging from small molecules to whole cells. High-resolution structures of RNA-aptamers in complex with their cognate ligands often reveal unexpected tertiary structure elements. Recent studies on different classes of aptamers binding the nucleotide triphosphate GTP as a ligand showed that these systems not only differ widely in binding affinity but also in their ligand binding modes and structural complexity. We initiated the NMR-based structure determination of the high-affinity binding GTP-aptamer 9-12 in order to gain further insights into the diversity of ligand binding modes and structural variability of those aptamers. Here, we report 1H, 13C and 15N resonance assignments for the GTP 9-12-aptamer bound to GTP as the prerequisite for the structure determination by solution NMR.


Subject(s)
Aptamers, Nucleotide/chemistry , Aptamers, Nucleotide/metabolism , Guanosine Triphosphate/metabolism , Nuclear Magnetic Resonance, Biomolecular , Aptamers, Nucleotide/genetics , Base Sequence
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