Ontology highlight
ABSTRACT:
SUBMITTER: Qureshi SH
PROVIDER: S-EPMC2731815 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Biochemistry 20090901 34
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 the Na(+)-binding site was stabilized by an engineered disulfide bond. This was possi ...[more]