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Latrophilin-1 (Lat-1), a target receptor for alpha-Latrotoxin, is a putative G protein-coupled receptor implicated in synaptic function. The extracellular portion of Lat-1 contains a rhamnose binding lectin (RBL)-like domain of unknown structure. RBL domains, first isolated from the eggs of marine species, are also found in the ectodomains of other metazoan transmembrane proteins, including a recently discovered coreceptor of the neuronal axon guidance molecule SLT-1/Slit. Here, we describe a structure of this domain from the mouse Lat-1. RBL adopts a unique alpha/beta fold with long structured loops important for monosaccharide recognition, as shown in the structure of a complex with L-rhamnose. Sequence alignments and mutagenesis show that residues important for carbohydrate binding are often absent in other receptor-attached examples of RBL, including the SLT-1/Slit coreceptor. We postulate that this domain class facilitates direct protein-protein interactions in many transmembrane receptors.

Original publication

DOI

10.1016/j.str.2008.02.020

Type

Journal article

Journal

Structure

Publication Date

06/2008

Volume

16

Pages

944 - 953

Keywords

Amino Acid Sequence, Amino Acid Substitution, Animals, Carbohydrates, Lectins, Mice, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Binding, Protein Structure, Tertiary, Receptors, G-Protein-Coupled, Receptors, Peptide, Rhamnose, Sequence Homology, Amino Acid, Solutions