Andersen, Olav M.3; Dagil, Robert4; Kragelund, Birthe Brandt4
1 Centre for Medical Parasitology, Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, Københavns Universitet2 Biomolecular Sciences, Department of Biology, Faculty of Science, Københavns Universitet3 Institut for Biomedicin - Forskning og uddannelse, Vest4 Biomolecular Sciences, Department of Biology, Faculty of Science, Københavns Universitet
communication by β-propellers
The lipoprotein receptor (LR) family constitutes a large group of structurally closely related receptors with broad ligand-binding specificity. Traditionally, ligand binding to LRs has been anticipated to involve merely the complement type repeat (CR)-domains omnipresent in the family. Recently, this dogma has transformed with the observation that β-propellers of some LRs actively engage in complex formation too. Based on an in-depth decomposition of current structures and sequences, we suggest that exploitation of the β-propellers as binding targets depends on receptor subgroups. In particular, we highlight the shutter mechanism of β-propellers as a general recognition motif for NxI-containing ligands, and we present indications that the generalized β-propeller-induced ligand release mechanism is not applicable for the larger LRs. For the giant LR members, we present evidence that their β-propellers may also actively engage in ligand binding. We therefore advocate for an increased focus on solving the structure-function relationship of this group of important biological receptors.
Journal of Lipid Research, 2013, Vol 54, p. 2763-2774