New horizons for lipoprotein receptors: communication by β-propellers
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New horizons for lipoprotein receptors : communication by β-propellers. / Andersen, Olav M.; Dagil, Robert; Kragelund, Birthe Brandt.
I: Journal of Lipid Research, Bind 54, 2013, s. 2763-2774.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - New horizons for lipoprotein receptors
T2 - communication by β-propellers
AU - Andersen, Olav M.
AU - Dagil, Robert
AU - Kragelund, Birthe Brandt
PY - 2013
Y1 - 2013
N2 - 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.
AB - 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.
U2 - 10.1194/jlr.M039545
DO - 10.1194/jlr.M039545
M3 - Journal article
C2 - 23881912
VL - 54
SP - 2763
EP - 2774
JO - Journal of Lipid Research
JF - Journal of Lipid Research
SN - 0022-2275
ER -
ID: 94396671