Structure of prothrombin in the closed form reveals new details on the mechanism of activation.

ABSTRACT: The clotting factor prothrombin exists in equilibrium between closed and open conformations, but the physiological role of these forms remains unclear. As for other allosteric proteins, elucidation of the linkage between molecular transitions and function is facilitated by reagents stabilized in each of the alternative conformations. The open form of prothrombin has been characterized structurally, but little is known about the architecture of the closed form that predominates in solution under physiological conditions. Using X-ray crystallography and single-molecule FRET, we characterize a prothrombin construct locked in the closed conformation through an engineered disulfide bond. The construct: (i) provides structural validation of the intramolecular collapse of kringle-1 onto the prote

SUBMITTER: Chinnaraj M 

PROVIDER: S-EPMC5811608 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature