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2fhw

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fhw OCA], [http://www.ebi.ac.uk/pdbsum/2fhw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fhw RCSB]</span>
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[[Category: insulin/relaxin super-family fold]]
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Revision as of 00:03, 31 March 2008


PDB ID 2fhw

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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