The structure of vitellogenin provides a molecular model for the assembly and secretion of atherogenic lipoproteins
Mann,C.J.; Anderson,T.A.; Read,J.; Chester,S.A.; Harrison,G.B.; Kochl,S.; Ritchie,P.J.; Bradbury,P.; Hussain,F.S.; Amey,J.; Vanloo,B.; Rosseneu,M.; Infante,R.; Hancock,J.M.; Levitt,D.G.; Banaszak,L.J.; Scott,J.; Shoulders,C.C.;
The assembly of atherogenic lipoproteins requires the formation in the endoplasmic reticulum of a complex between apolipoprotein (apo)B, a microsomal triglyceride transfer protein (MTP) and protein disulphide isomerase (PDI). Here we show by molecular modelling and mutagenesis that the globular amino-terminal regions of apoB and MTP are closely related in structure to the ancient egg yolk storage protein, vitellogenin (VTG).
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