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- W4385331316 abstract "Abstract Ligand/protein molecular recognition involves a dynamic process, whereby both partners require a degree of structural plasticity to regulate the binding/unbinding event. Here, we present the characterization of the interaction between a highly dynamic G-rich oligonucleotide, M08s-1, and its target protein, human α-thrombin. M08s-1 is the most active anticoagulant aptamer selected thus far. Circular dichroism and gel electrophoresis analyses indicate that both intramolecular and intermolecular G-quadruplex structures are populated in solution. The presence of thrombin stabilises the antiparallel intramolecular chair-like G-quadruplex conformation, that provides by far the main contribution to the biological activity of the aptamer. The crystal structure of the thrombin-oligonucleotide complex reveals that M08s-1 adopts a kinked structural organization formed by a G-quadruplex domain and a long duplex module, linked by a stretch of five purine bases. The quadruplex motif hooks the exosite I region of thrombin and the duplex region is folded towards the surface of the protein. This structural feature, which has never been observed in other anti-exosite I aptamers with a shorter duplex motif, hinders the approach of a protein substrate to the active site region and may well explain the significant increase in the anticoagulant activity of M08s-1 compared to the other anti-exosite I aptamers." @default.
- W4385331316 created "2023-07-29" @default.
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- W4385331316 date "2023-07-28" @default.
- W4385331316 modified "2023-10-06" @default.
- W4385331316 title "Steric hindrance and structural flexibility shape the functional properties of a guanine-rich oligonucleotide" @default.
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- W4385331316 doi "https://doi.org/10.1093/nar/gkad634" @default.
- W4385331316 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37503836" @default.
- W4385331316 hasPublicationYear "2023" @default.
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