Crystal structure of the class V GTP-binding RNA aptamer bound to its ligand: GTP recognition by a topologically complex intermolecular G-quadruplex.

ABSTRACT: RNA aptamers obtained from in vitro selection experiments provide unique insights into the structural properties and ligand recognition capabilities of RNA in general. In order to investigate the relationships between RNA sequence information content and structural complexity with ligand affinity and specificity, the Szostak group previously identified eleven different families of GTP-binding aptamers varying widely in their sequence conservation patterns as well as in their secondary structure complexity and topology. The class V GTP aptamer has a particularly high affinity for GTP. Here, we report the high-resolution X-ray crystal structure of this aptamer-GTP complex. Remarkably, GTP is found to be integrated into one layer of a two-layered G-quadruplex, thereby rationalizing the high l

SUBMITTER: Stafflinger H 

PROVIDER: S-EPMC12718690 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature