Modeling the primary hormone-binding site of RXFP1 and RXFP2

DJ Scott; GW Tregear; RAD Bathgate

Conference Proceedings

Modeling the primary hormone-binding site of RXFP1 and RXFP2

DJ Scott, GW Tregear, RAD Bathgate

Annals of the New York Academy of Sciences | WILEY-BLACKWELL | Published : 2009

DOI: 10.1111/j.1749-6632.2009.03950.x

Abstract

The primary binding sites of the relaxin and insulin-like peptide 3 (INSL3) receptors, RXFP1 and RXFP2, are found within the leucine-rich repeats (LRRs) of the ectodomains. Specific B-chain residues in the peptides interact with residues in the inner β-sheets of the LRRs of the receptors. Relaxin binds to RXFP2 with high affinity, although INSL3 has a very poor affinity for RXFP1. In this paper we present evidence that relaxin binds to the LRRs of RXFP2 in a manner similar to INSL3 binding to its receptor. Additionally, we introduce a model of this binding interaction and compare it to an alternate model for relaxin-RXFP1 binding. © 2009 New York Academy of Sciences.

University of Melbourne Researchers

Daniel Scott Author

Ross Bathgate Author

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Grants

Awarded by National Health and Medical Research Council of Australia (NHMRC)

Funding Acknowledgements

Ross Bathgate is the recipient of a Senior Research Fellowship, Daniel Scott is the recipient of a CJ Martin Fellowship, and Geoff Tregear is the recipient of a Senior Principle Research Fellowship from the National Health and Medical Research Council of Australia (NHMRC). This work was supported by project grants 300012 and 454375 from the NHMRC.