Journal article
The Structural and Functional Role of the B-chain C-terminal Arginine in the Relaxin-3 Peptide Antagonist, R3(B Delta 23-27)R/I5
Mohammed Akhter Hossain, Ross AD Bathgate, K Johan Rosengren, Fazel Shabanpoor, Suode Zhang, Feng Lin, Geoffrey W Tregear, John D Wade
CHEMICAL BIOLOGY & DRUG DESIGN | WILEY | Published : 2009
Abstract
Relaxin-3, a member of the insulin superfamily, is involved in regulating stress and feeding behavior. It is highly expressed in the brain and is the endogenous ligand for the receptor RXFP3. As relaxin-3 also interacts with the relaxin receptor RXFP1, selective agonists and antagonists are crucial for studying the physiological function(s) of the relaxin-3/RXFP3 pair. The analog R3(BDelta23-27)R/I5, in which a C-terminally truncated human relaxin-3 (H3) B-chain is combined with the INSL5 A-chain, is a potent selective RXFP3 antagonist and has an Arg residue remaining on the B-chain C-terminus as a consequence of the recombinant protein production process. To investigate the role of this res..
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Grants
Awarded by National Health and Medical Research Council of Australia Project
Funding Acknowledgements
We thank Tania Ferraro for help with the binding assays and Linda Chan for the amino acid analyses. This work was funded by National Health and Medical Research Council of Australia Project grants # 350 284 and 508 995 to J. D. W., R. A. D. B. and G. W. T.