2fhw
From Proteopedia
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
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Solution structure of human relaxin-3
Overview
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.
About this Structure
2FHW is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3., Rosengren KJ, Lin F, Bathgate RA, Tregear GW, Daly NL, Wade JD, Craik DJ, J Biol Chem. 2006 Mar 3;281(9):5845-51. Epub 2005 Dec 19. PMID:16365033
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