Structure of the Transmembrane Signal Initiation Site of the Relaxin-Like Factor (RLF/INSL3)

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 s...

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Bibliographic Details
Published in:Biochemistry (Easton) 2007-08, Vol.46 (34), p.9722-9727
Main Authors: Büllesbach, Erika E, Schwabe, Christian
Format: Article
Language:English
Subjects:
Cell Membrane - physiology
Cells, Cultured
Cyclic AMP - metabolism
Humans
Insulin - chemistry
Insulin - genetics
Insulin - metabolism
Peptide Fragments - chemistry
Peptide Fragments - genetics
Peptide Fragments - metabolism
Protein Sorting Signals - physiology
Proteins - chemistry
Proteins - genetics
Proteins - metabolism
Receptors, G-Protein-Coupled - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi700708s