Ontology highlight
ABSTRACT:
SUBMITTER: Fuglestad B
PROVIDER: S-EPMC3808083 | biostudies-literature | 2013 Oct
REPOSITORIES: biostudies-literature
Fuglestad Brian B Gasper Paul M PM McCammon J Andrew JA Markwick Phineus R L PR Komives Elizabeth A EA
The journal of physical chemistry. B 20130528 42
Thrombin is the central protease in the cascade of blood coagulation proteases. The structure of thrombin consists of a double β-barrel core surrounded by connecting loops and helices. Compared to chymotrypsin, thrombin has more extended loops that are thought to have arisen from insertions in the serine protease that evolved to impart greater specificity. Previous experiments showed thermodynamic coupling between ligand binding at the active site and distal exosites. We present a combined appro ...[more]