Ontology highlight
ABSTRACT:
SUBMITTER: Emmanouilidis L
PROVIDER: S-EPMC5353646 | biostudies-literature | 2017 Mar
REPOSITORIES: biostudies-literature
Nature communications 20170310
The transport of peroxisomal membrane proteins (PMPs) requires the soluble PEX19 protein as chaperone and import receptor. Recognition of cargo PMPs by the C-terminal domain (CTD) of PEX19 is required for peroxisome biogenesis in vivo. Farnesylation at a C-terminal CaaX motif in PEX19 enhances the PMP interaction, but the underlying molecular mechanisms are unknown. Here, we report the NMR-derived structure of the farnesylated human PEX19 CTD, which reveals that the farnesyl moiety is buried in ...[more]