Ceramide-1-phosphate transfer protein promotes sphingolipid reorientation needed for binding during membrane interaction.

ABSTRACT: Lipid transfer proteins acquire and release their lipid cargoes by interacting transiently with source and destination biomembranes. In the GlycoLipid Transfer Protein (GLTP) superfamily, the two-layer all-α-helical GLTP-fold defines proteins that specifically target sphingolipids (SLs) containing either sugar or phosphate headgroups via their conserved but evolutionarily-modified SL recognitions centers. Despite comprehensive structural insights provided by X-ray crystallography, the conformational dynamics associated with membrane interaction and SL uptake/release by GLTP superfamily members have remained unknown. Herein, we report insights gained from molecular dynamics (MD) simulations into the conformational dynamics that enable ceramide-1-phosphate transfer proteins (CPTPs) to acquir

SUBMITTER: Gao YG 

PROVIDER: S-EPMC8953657 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature