The intra-A-chain disulfide bond of INSL3 was essential for RXFP2 receptor binding and activation, revealing structural requirements for this reproductive peptide's function in fertility and testicular descent.
Key findingThe intra-A-chain disulfide bond of INSL3 was essential for RXFP2 receptor binding and activation, revealing structural requirements for this reproduc
What the researchers found
The intra-A-chain disulfide bond of INSL3 was essential for RXFP2 receptor binding and activation, revealing structural requirements for this reproductive peptide's function in fertility and testicular descent.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2010.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2.
Peptides, 31(9), 1730-6
Citation
Zhang, Suode; Hughes, Richard A; Bathgate, Ross A D; Shabanpoor, Fazel; Hossain, M Akhter; Lin, Feng; van Lierop, Bianca; Robinson, Andrea J; Wade, John D. (2010). Role of the intra-A-chain disulfide bond of insulin-like peptide 3 in binding and activation of its receptor, RXFP2.. Peptides, 31(9), 1730-6. https://doi.org/10.1016/j.peptides.2010.05.021