| http://purl.uniprot.org/citations/18434306 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18434306 | http://www.w3.org/2000/01/rdf-schema#comment | "The relaxin peptides are a family of hormones that share a structural fold characterized by two chains, A and B, that are cross-braced by three disulfide bonds. Relaxins signal through two different classes of G-protein-coupled receptors (GPCRs), leucine-rich repeat-containing GPCRs LGR7 and LGR8 together with GPCR135 and GPCR142, now referred to as the relaxin family peptide (RXFP) receptors 1-4, respectively. Although key binding residues have been identified in the B-chain of the relaxin peptides, the role of the A-chain in their activity is currently unknown. A recent study showed that INSL3 can be truncated at the N terminus of its A-chain by up to 9 residues without affecting the binding affinity to its receptor RXFP2 while becoming a high affinity antagonist. This suggests that the N terminus of the INSL3 A-chain contains residues essential for RXFP2 activation. In this study, we have synthesized A-chain truncated human relaxin-2 and -3 (H2 and H3) relaxin peptides, characterized their structure by both CD and NMR spectroscopy, and tested their binding and cAMP activities on RXFP1, RXFP2, and RXFP3. In stark contrast to INSL3, A-chain-truncated H2 relaxin peptides lost RXFP1 and RXFP2 binding affinity and concurrently cAMP-stimulatory activity. H3 relaxin A-chain-truncated peptides displayed similar properties on RXFP1, highlighting a similar binding mechanism for H2 and H3 relaxin. In contrast, A-chain-truncated H3 relaxin peptides showed identical activity on RXFP3, highlighting that the B-chain is the sole determinant of the H3 relaxin-RXFP3 interaction. Our results provide new insights into the action of relaxins and demonstrate that the role of the A-chain for relaxin activity is both peptide- and receptor-dependent."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m801911200"xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Zhang S."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Rosengren K.J."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Hossain M.A."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Ferraro T."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Daly N.L."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Wade J.D."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Tregear G.W."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Layfield S."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Bathgate R.A."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/author | "Haugaard-Jonsson L.M."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/pages | "17287-17297"xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/title | "The A-chain of human relaxin family peptides has distinct roles in the binding and activation of the different relaxin family peptide receptors."xsd:string |
| http://purl.uniprot.org/citations/18434306 | http://purl.uniprot.org/core/volume | "283"xsd:string |
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