Abstract
The thrombin-binding aptamer (TBA) is a consensus DNA 15-mer that binds specifically to human-thrombin at nanomolar concentrations and inhibits its procoagulant functions. Recently, a modified TBA (mTBA) containing a 5′-5′ inversion-of-polarity site has been shown to be more stable and to possess a higher thrombin affinity than its unmodified counterpart. The structure of the thrombin-TBA complex has previously been determined at low resolution, but did not provide a detailed picture of the aptamer conformation or of the protein-DNA assembly, while that of the complex with mTBA is unknown. Crystallographic analysis of the thrombin-mTBA complex has been attempted. The crystals diffracted to 2.15 Å resolution and belonged to space group I222. © 2010 International Union of Crystallography All rights reserved.
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Russo Krauss, I., Merlino, A., Randazzo, A., Mazzarella, L., & Sica, F. (2010). Crystallization and preliminary X-ray analysis of the complex of human α-thrombin with a modified thrombin-binding aptamer. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(8), 961–963. https://doi.org/10.1107/S1744309110024632
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