Journal article

Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function

Y Yan, DJ Scott, TN Wilkinson, J Ji, GW Tregear, RAD Bathgate

Biochemistry | AMER CHEMICAL SOC | Published : 2008

Abstract

The relaxin receptor, RXFP1, is a member of the leucine-rich repeat-containing G-protein-coupled receptor (LGR) family. These receptors are characterized by a large extracellular ectodomain containing leucine-rich repeats which contain the primary ligand binding site. RXFP1 contains six putative Asn-linked glycosylation sites in the ectodomain at positions Asn-14, Asn-105, Asn-242, Asn-250, Asn-303, and Asn-346, which are highly conserved across species. N-Linked glycosylation is the most common post-translational modification of G-protein-coupled receptors, although its role in modulating receptor function differs. We herein investigate the actual N-linked glycosylation status of RXFP1 and ..

View full abstract

University of Melbourne Researchers