Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2

S Zhang; RA Hughes; RAD Bathgate; F Shabanpoor; MA Hossain; F Lin; B Van Lierop; AJ Robinson; JD Wade

Journal article

Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2

S Zhang, RA Hughes, RAD Bathgate, F Shabanpoor, MA Hossain, F Lin, B Van Lierop, AJ Robinson, JD Wade

Peptides | Published : 2010

DOI: 10.1016/j.peptides.2010.05.021

Abstract

INSL3 is a member of the insulin-IGF-relaxin superfamily and plays a key role in male fetal development and in adult germ cell maturation. It is the cognate ligand for RXFP2, a leucine-rich repeat containing G-protein coupled receptor. To date, and in contrast to our current knowledge of the key structural features that are required for the binding of INSL3 to RXFP2, comparatively little is known about the key residues that are required to elicit receptor activation and downstream cell signaling. Early evidence suggests that these are contained principally within the A-chain. To further explore this hypothesis, we have undertaken an examination of the functional role of the intra-A-chain dis..

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University of Melbourne Researchers

Ross Bathgate Author

Akhter Hossain Author

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Grants

Awarded by National Health and Medical Research Council

Funding Acknowledgements

This work was funded by National Health and Medical Research Council of Australia Project grants #350245 and 509048 to JDW, RADB and RAH. We thank Linda Chan for the amino acid analyses and Tania Ferraro and Sharon Layfield for performing binding and cAMP assays.