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- W2004514863 abstract "We have discovered the signal initiation structure of the relaxin-like factor and shown its function to be independent of the amino acid side chains in the contact region. Evidence presented in this article suggests that signal induction is a function of the peptide bond and that completion of the signaling contact is initiated by ligand binding to the leucine-rich repeat G-protein coupled receptor 8 (LGR8). The specific mode of binding forces certain peptide bonds into a signaling position. This observation implies that the receiving structures are equally nonspecific so that signaling should occur at any peptide bond of the receptor or the trans-membrane loop that is within reach of the signaling wires of the receptor-bound ligand. Our observations offer an explanation for ligand cross-talk as well as for the ability of some antibodies to elicit the biological response normally associated with a specific ligand." @default.
- W2004514863 created "2016-06-24" @default.
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- W2004514863 date "2007-08-01" @default.
- W2004514863 modified "2023-10-18" @default.
- W2004514863 title "Structure of the Transmembrane Signal Initiation Site of the Relaxin-Like Factor (RLF/INSL3)" @default.
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- W2004514863 doi "https://doi.org/10.1021/bi700708s" @default.
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