Crystallization and preliminary X-ray analysis of the complex of human alpha-thrombin with a modified thrombin-binding aptamer.
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.
Russo Krauss
Irene
I
Dipartimento di Chimica, Università di Napoli Federico II, Via Cintia, I-80126 Napoli, Italy.
Merlino
Antonello
A
Randazzo
Antonio
A
Mazzarella
Lelio
L
Sica
Filomena
F
D052157:Aptamers, Nucleotide / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D011485:Protein Binding; D055503:Protein Multimerization; D013917:Thrombin / Q000737:chemistry* / Q000378:metabolism
D052157:Aptamers, Nucleotide; C081676:thrombin aptamer; D013917:Thrombin