Journal article

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

Shoni Bruell, Ashish Sethi, Nicholas Smith, Daniel J Scott, Mohammed Akhter Hossain, Qing-Ping Wu, Zhan-Yun Guo, Emma J Petrie, Paul R Gooley, Ross AD Bathgate

SCIENTIFIC REPORTS | NATURE PUBLISHING GROUP | Published : 2017

Abstract

Relaxin family peptide receptor 2 (RXFP2) is a GPCR known for its role in reproductive function. It is structurally related to the human relaxin receptor RXFP1 and can be activated by human gene-2 (H2) relaxin as well as its cognate ligand insulin-like peptide 3 (INSL3). Both receptors possess an N-terminal low-density lipoprotein type a (LDLa) module that is necessary for activation and is joined to a leucine-rich repeat domain by a linker. This linker has been shown to be important for H2 relaxin binding and activation of RXFP1 and herein we investigate the role of the equivalent region of RXFP2. We demonstrate that the linker's highly-conserved N-terminal region is essential for activatio..

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Grants

Awarded by National Health and Medical Research Council of Australia


Awarded by Australian Research Council


Funding Acknowledgements

The authors thank Tania Ferraro and Sharon Layfield for technical assistance. This research was supported by National Health and Medical Research Council of Australia project grants [1043750] and [1100676] (RADB and PRG), the Victorian Government Operational Infrastructure Support Program and equipment grants from the Australian Research Council [LE120100022]. RADB is supported by an NHMRC Research Fellowship.