Atomistic characterization of β2-glycoprotein I domain V interaction with anionic membranes.

ABSTRACT:

Background

Interaction of β₂-glycoprotein I (β₂GPI) with anionic membranes is crucial in antiphospholipid syndrome (APS), implicating the role of its membrane-binding domain, domain V (DV). The mechanism of DV binding to anionic lipids is not fully understood.

Objectives

This study aimed to elucidate the molecular details of β₂GPI DV binding to anionic membranes.

Methods

We utilized molecular dynamics simulations to investigate the structural basis of anionic lipid recognition by DV. To corroborate the membrane-binding mode identified in the highly mobile membrane mimetic simulations, we conducted additional simulations using a full membrane model.

Results

The study identified critical regions in DV, namely the lysine-rich loop

SUBMITTER: Hasdemir HS 

PROVIDER: S-EPMC11992691 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature