Structural plasticity in the loop region of engineered lipocalins with novel ligand specificities, so-called Anticalins.

ABSTRACT: Anticalins are generated via combinatorial protein design on the basis of the lipocalin protein scaffold and constitute a novel class of small and robust engineered binding proteins that offer prospects for applications in medical therapy as well as in vivo diagnostics as an alternative to antibodies. The lipocalins are natural binding proteins with diverse ligand specificities which share a simple architecture with a central eight-stranded antiparallel β-barrel and an α-helix attached to its side. At the open end of the β-barrel, four structurally variable loops connect the β-strands in a pair-wise manner and, together, shape the ligand pocket. Using targeted random mutagenesis in combination with molecular selection techniques, this loop region can be reshaped to generate pockets

SUBMITTER: Achatz S 

PROVIDER: S-EPMC8693463 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature