Journal article
C-terminus of the B-chain of relaxin-3 is important for receptor activity
F Shabanpoor, RAD Bathgate, JD Wade, MA Hossain
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2013
Abstract
Human relaxin-3 is a neuropeptide that is structurally similar to human insulin with two chains (A and B) connected by three disulfide bonds. It is expressed primarily in the brain and has modulatory roles in stress and anxiety, feeding and metabolism, and arousal and behavioural activation. Structure-activity relationship studies have shown that relaxin-3 interacts with its cognate receptor RXFP3 primarily through its B-chain and that its A-chain does not have any functional role. In this study, we have investigated the effect of modification of the B-chain C-terminus on the binding and activity of the peptide. We have chemically synthesised and characterized H3 relaxin as C-termini acid (b..
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Grants
Awarded by National Health and Medical Research Council
Funding Acknowledgements
This research was partially funded by NHMRC (Australia) project grants 508995, and 1023078 to JDW, MAH and RADB. Research at the Florey Institute of Neuroscience and Mental Health is supported by the Victorian Government Operational Infrastructure Support Program. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.