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Crystallization and preliminary X-ray analysis of the complex of human alpha-thrombin with a modified thrombin-binding aptamer

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):961-3. doi: 10.1107/S1744309110024632. Epub 2010 Jul 29.

Abstract

The thrombin-binding aptamer (TBA) is a consensus DNA 15-mer that binds specifically to human alpha-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 A resolution and belonged to space group I222.

MeSH terms

  • Aptamers, Nucleotide / chemistry*
  • Aptamers, Nucleotide / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Humans
  • Protein Binding
  • Protein Multimerization*
  • Thrombin / chemistry*
  • Thrombin / metabolism

Substances

  • Aptamers, Nucleotide
  • thrombin aptamer
  • Thrombin