title: New horizons for lipoprotein receptors: communication by β-propellers.
abstract: 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.
authors.affiliation: Department of Biomedicine, Aarhus University, DK-8000 Aarhus C, Denmark; and.
authors.forename: Olav M
authors.initials: OM
authors.lastname: Andersen
authors.forename: Robert
authors.initials: R
authors.lastname: Dagil
authors.forename: Birthe B
authors.initials: BB
authors.lastname: Kragelund
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary; D018110:Receptors, Lipoprotein / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction; D040681:Structural Homology, Protein
chemical_list: D018110:Receptors, Lipoprotein
keywords: Tyr-Trp-Thr-Asp β-propeller; endocytosis; internalisation; ligand recognition motif; ligand release; structure