Article
Mutagenesis studies toward understanding allostery in thrombin.
Biochemistry - 1 Sept 2009
Qureshi Shabir H, Yang Likui, Manithody Chandrashekhara, Iakhiaev Alexei V, Rezaie Alireza R
Abstract excerpt
The binding of thrombomodulin (TM) to exosite-1 and the binding of Na(+) to 225-loop allosterically modulate the catalytic activity and substrate specificity of thrombin. To determine whether the conformation of these two cofactor-binding loops are energetically linked to each other and to the active site, we rationally designed two thrombin mutants in which either the 70-80 loop of exosite-1 or the 225-loop of...
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