The J-elongated conformation of β₂-glycoprotein I predominates in solution: implications for our understanding of antiphospholipid syndrome.

ABSTRACT: β₂-Glycoprotein I (β₂GPI) is an abundant plasma protein displaying phospholipid-binding properties. Because it binds phospholipids, it is a target of antiphospholipid antibodies (aPLs) in antiphospholipid syndrome (APS), a life-threatening autoimmune thrombotic disease. Indeed, aPLs prefer membrane-bound β₂GPI to that in solution. β₂GPI exists in two almost equally populated redox states: oxidized, in which all the disulfide bonds are formed, and reduced, in which one or more disulfide bonds are broken. Furthermore, β₂GPI can adopt multiple conformations (i.e. J-elongated, S-twisted, and O-circular). While strong evidence indicates that the J-form is the structure bound to aPLs, which conformation exists and predominates in solu

SUBMITTER: Ruben E 

PROVIDER: S-EPMC7397106 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature