Solution Structure and Novel Insights into the Determinants of the Receptor Specificity of Human Relaxin-3.
From: Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia.
The Journal of biological chemistry
- Publish Date: Mar 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 9
- Pages: 5845-51
- Medium: Print
- Language: English
- Citation (JAMA): Rosengren K Johan, Lin Feng, Bathgate Ross A D, et al. Solution Structure and Novel Insights into the Determinants of the Receptor Specificity of Human Relaxin-3.. J. Biol. Chem. Mar 2006;281:5845-51
Abstract
Relaxin-3 is the most recently discovered member of the relaxin family of peptide hormones. In contrast to relaxin-1 and -2, whose main functions are associated with pregnancy, relaxin-3 is involved in neuropeptide signaling in the brain. Here, we report the solution structure of human relaxin-3, the first structure of a relaxin family member to be solved by NMR methods. Overall, relaxin-3 adopts an insulin-like fold, but the structure differs crucially from the crystal structure of human relaxin-2 near the B-chain terminus. In particular, the B-chain C terminus folds back, allowing Trp(B27) to interact with the hydrophobic core. This interaction partly blocks the conserved RXXXRXXI motif identified as a determinant for the interaction with the relaxin receptor LGR7 and may account for the lower affinity of relaxin-3 relative to relaxin for this receptor. This structural feature is likely important for the activation of its endogenous receptor, GPCR135.
Mesh Headings (Keywords): Amino Acid Sequence, Animals, Binding Sites, Cell Line, Cyclic AMP, Female, Humans, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Pregnancy, Protein Folding, Protein Structure, Secondary, Receptors, G-Protein-Coupled, Relaxin, Sequence Alignment
Check for Full Text / PubMed Unique Identifier (PMID): 16365033
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