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Rosengren, K.J. et al.

Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3.

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.[1]

References

Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3. Rosengren, K.J., Lin, F., Bathgate, R.A., Tregear, G.W., Daly, N.L., Wade, J.D., Craik, D.J. J. Biol. Chem. (2006) [Pubmed]

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