Distinct activation modes of the Relaxin Family Peptide Receptor 2 in response to insulin-like peptide 3 and relaxin.

摘要: Relaxin family peptide receptor 2 (RXFP2) is a GPCR known for its role in reproductive function. It structurally related to the human relaxin RXFP1 and can be activated by gene-2 (H2) as well cognate ligand insulin-like 3 (INSL3). Both receptors possess an N-terminal low-density lipoprotein type (LDLa) module that necessary activation joined leucine-rich repeat domain linker. This linker has been shown important H2 binding of herein we investigate equivalent region RXFP2. We demonstrate linker's highly-conserved essential RXFP2 response both ligands. In contrast, relaxin, but not INSL3, binding. Our results highlight distinct mechanism which INSL3 activates whereby mediates reorientation LDLa activate transmembrane domains conjunction with A-chain. involves more RXFP1-like involving LDLa-linker, alone.