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. 2018 Aug 21;293(41):15765–15776. doi: 10.1074/jbc.RA118.002611

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© 2018 Haugaard-Kedström et al.

Published under exclusive license by The American Society for Biochemistry and Molecular Biology, Inc.

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Figure 1. — Structure and receptor-interacting amino acid residues of relaxin-3. The A-chain, shown in gray, consists of two antiparallel helices connected by a β-strand. The B-chain, shown in green, comprises a helical segment spanning from Gly¹¹ to Cys²². Disulfides are shown in yellow. Side chains important for binding to RXFP3 and for activating RXFP3 are shown in blue and red, respectively. The R3 B1-22R antagonist retains only the B-chain with the two cysteines at positions 10 and 22 replaced with Ser and the C-terminal five amino acid residues 23–27 replaced with a nonnative Arg²³.