The large subunit of MTP, also known as the alpha subunit, contains an N-terminal half
beta barrel, an alpha helix and a C-terminal lipid binding site that lies between two
beta pleated sheets. It is a member of the
large lipid transfer protein family, like
apolipoprotein B (apo B), with which it interacts, but unlike apo B, it is not secreted. The heterodimer is instead retained in the endoplasmic reticulum due to the presence of a C-terminal
KDEL motif on the PDI beta subunit. ==Interactive pathway map==