A High-Throughput Small-Angle X-ray Scattering Assay to Determine the Conformational Change of Plasminogen.

ABSTRACT: Plasminogen (Plg) is the inactive form of plasmin (Plm) that exists in two major glycoforms, referred to as glycoforms I and II (GI and GII). In the circulation, Plg assumes an activation-resistant "closed" conformation via interdomain interactions and is mediated by the lysine binding site (LBS) on the kringle (KR) domains. These inter-domain interactions can be readily disrupted when Plg binds to lysine/arginine residues on protein targets or free L-lysine and analogues. This causes Plg to convert into an "open" form, which is crucial for activation by host activators. In this study, we investigated how various ligands affect the kinetics of Plg conformational change using small-angle X-ray scattering (SAXS). We began by examining the open and closed conformations of Plg using size-exclu

SUBMITTER: Quek AJ 

PROVIDER: S-EPMC10531915 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature