Literature summary for 3.4.21.5 extracted from

Dolot, R.; Lam, C.H.; Sierant, M.; Zhao, Q.; Liu, F.W.; Nawrot, B.; Egli, M.; Yang, X.
Crystal structures of thrombin in complex with chemically modified thrombin DNA aptamers reveal the origins of enhanced affinity (2018), Nucleic Acids Res., 46, 4819-4830 .

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Application

Application	Comment	Organism
medicine	because of the essential role of thrombin in the coagulation cascade, achieving the ability to specifically modulate thrombin activity represents a major goal in the development of anticoagulant strategies. Thrombin-binding aptamer (TBA), is a single-stranded 15-mer DNA with the sequence (5'-GGT TGG TGT GGT TGG-3') that binds thrombin with high specificity and affinity. TBA specifically inhibits clot-bound thrombin and reduces arterial thrombus formation. Native TBA consisting of only natural bases is susceptible to nuclease digestion and has a very short half-life in vivo of 108/s. Its binding affinity and selectivity need to be optimized. These optimization efforts are of critical importance in both diagnostic and therapeutic applications. Chemical modification of the DNA aptamer can be used to significantly improve its binding affinity	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of thrombin in complex with chemically modified thrombin DNA aptamers	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P00734	-	-

General Information

General Information	Comment	Organism
physiological function	the enzyme plays a key role in blood coagulation	Homo sapiens

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Release 2023.1 (January 2023)