10.80082/42451F59-D687-49DC-B3E5-4FAB2F51D2E7
Naschberger, Andreas
Andreas
Naschberger
PHINERA, Yannick
Yannick
PHINERA
Bowler, Matthew W.
Matthew W.
Bowler
Rupp, Bernhard
Bernhard
Rupp
DataCite Metadata Schema Documentation for the Publication and Citation of Research Data v4.0
title 2 by sapo
DataCite e.V.
2016
Datacollection
OPID-1
PUMA
Afamin, a human plasma glycoprotein and putative transporter of hydrophobic molecules, has been shown to act as extracellular chaperone for poorly soluble, acylated Wnt proteins, forming a stable, soluble complex with functioning Wnt proteins. The 2.1-Å crystal structure of glycosylated human afamin reveals an almost exclusively hydrophobic binding cleft capable of harboring large hydrophobic moieties. Lipid analysis confirms the presence of lipids, and density in the primary binding pocket of afamin was modeled as palmitoleic acid, presenting the native O-acylation on serine 209 in human Wnt3a. The modeled complex between the experimental afamin structure and a Wnt3a homology model based on the XWnt8-Fz8-CRD fragment complex crystal structure is compelling, with favorable interactions comparable with the crystal structure complex. Afamin readily accommodates the conserved palmitoylated serine 209 of Wnt3a, providing a structural basis how afamin solubilizes hydrophobic and poorly soluble Wnt proteins.