A complex between HLA-DR3 and a fragment of invariant chain called CLI
P was isolated from a human cell line defective in antigen presentatio
n and its X-ray crystal structure determined. Previous data indicate t
hat this complex is an intermediate in class II histocompatibility mat
uration, occurring between invariant chain-DR3 and antigenic peptide-D
R3 complexes. The structure shows that the CLIP fragment binds to DR3
in a way almost identical to that in which antigenic peptides bind cla
ss II histocompatibility glycoproteins. The structure is the substrate
for the loading of antigenic peptides by an exchange process catalyse
d by DM.