Structure and activity in the relaxin family of peptides

GW Tregear; RAD Bathgate; MA Hossain; F Lin; S Zhang; F Shabanpoor; DJ Scott; S Ma; AL Gundlach; CS Samuel; JD Wade

Journal article

Structure and activity in the relaxin family of peptides

GW Tregear, RAD Bathgate, MA Hossain, F Lin, S Zhang, F Shabanpoor, DJ Scott, S Ma, AL Gundlach, CS Samuel, JD Wade

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

DOI: 10.1111/j.1749-6632.2009.03955.x

Abstract

The availability of improved peptide synthesis procedures, convenient and sensitive assays for receptor binding and activation, together with advances in methods for structural characterization, has enabled the key structural features of the relaxin family of peptides responsible for biological activity to be defined. Not surprisingly, despite the similarities in primary amino acid sequences, different structural domains and residues are involved in the binding and activation at the four known relaxin family peptide receptors (RXFP1 to -4). Most of our knowledge on structure and function relates to the relaxin-RXFP1, insulin-like peptide 3 (INSL3)-RXFP2, and relaxin-3-RXFP3 systems, with inf..

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University of Melbourne Researchers

Ross Bathgate Author

Akhter Hossain Author

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Grants

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

Funding Acknowledgements

Geoffrey Tregear is a Senior Principal Research Fellow, John Wade is a Principle Research Fellow, and Ross Bathgate and Andrew Gundlach are Senior Research Fellows of the National Health & Medical Research Council of Australia (NHMRC). Chrishan Samuel is the recipient of a National Heart Foundation of Australia/NHMRC R.D. Wright Fellowship, and Sherie Ma is an NHMRC Australian Biomedical Postdoctoral Fellow This work was supported by project grants 300012, 454375, 508995, 509048, and 509246 from the NHMRC.