In the present work, the structure and function of ten human members of the lipocalin protein family as well as of one bacterial lipocalin were studied. At first, an expression system for their production under standardized conditions was established in E. coli. During the following analysis of their ligand-binding behaviour, the recombinant lipocalins exhibited similar properties as lipocalins from natural sources, even though some of them lack their natural glycosylation. The crystallographic analysis of some of the lipocalins, in particular of human tear lipocalin (Tlc) and C8γ, confirmed the typical lipocalin fold consisting of an eight-stranded β-barrel and a C-terminal α-helix. In the case of Tlc, interesting insight into the broad ligand-binding activity, which is caused by a bifurcated binding pocket as well as by conformational flexibility in the loop region at the entry, was obtained.     «

In the present work, the structure and function of ten human members of the lipocalin protein family as well as of one bacterial lipocalin were studied. At first, an expression system for their production under standardized conditions was established in E. coli. During the following analysis of their ligand-binding behaviour, the recombinant lipocalins exhibited similar properties as lipocalins from natural sources, even though some of them lack their natural glycosylation. The crystallographic...     »