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Binding of Na + to thrombin ensures high activity toward physiological substrates and optimizes the procoagulant and prothrombotic roles of the enzyme in vivo. Under physiological conditions of pH and temperature, the binding affinity of Na + is weak due to large heat capacity and enthalpy changes associated with binding, and the K d =80mM ensures only 64% saturation of the...
The thrombin mutant D221A/D222K (ARK) does not bind Na + and has interesting functional properties intermediate between those of the slow and fast forms of wild type. We solved the X-ray crystal structure of ARK bound at exosite I with a fragment of hirudin at 2.4-Å resolution. The structure shows a slight collapse of the 186 and 220 loops into the Na + binding site due to disruption...
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