An allosteric redox switch in domain V of β₂-glycoprotein I controls membrane binding and anti-domain I autoantibody recognition.

ABSTRACT: β₂-glycoprotein I (β₂GPI) is an abundant multidomain plasma protein that plays various roles in the clotting and complement cascades. It is also the main target of antiphospholipid antibodies (aPL) in the acquired coagulopathy known as antiphospholipid syndrome (APS). Previous studies have shown that β₂GPI adopts two interconvertible biochemical conformations, oxidized and reduced, depending on the integrity of the disulfide bonds. However, the precise contribution of the disulfide bonds to β₂GPI structure and function is unknown. Here, we substituted cysteine residues with serine to investigate how the disulfide bonds C32-C60 in domain I (DI) and C288-C326 in domain V (DV) regulate β₂GPI's structure and function. Results of our biophy

SUBMITTER: Kumar S 

PROVIDER: S-EPMC8326733 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature