Nature research paper: Structural basis for the tethered peptide activation of adhesion GPCRs
, Close-up view of the interactions of the β strand in thecomplex. The upper β strand formed substantial interactions with ECL3, including the hydrophobic packing of V554 and L558 in the β-strand contacts with V780, respectively, as well as the hydrogen bonds anchored between Y789 and H562. Hydrogen bonds are highlighted by blue dashed lines.sequence with ECL2 in GPR114-CTF-G, ELISA data to determine the cell surface expression levels of WT GPR133-CTF or mutants of thesequence in HEK293 cells.
Extended Data Fig. 6 Related expression and signaling data of GPR133 and GPR114 receptor and peptide mutants., ELISA data to determine the cell surface expression levels of WT GPR133-CTF or mutants of the binding pocket in HEK293 cells. The x-axis shows the amount of transfected DNA. The y-axis shows the ratio of corresponding receptor expression levels compared with the expression level of the WT GPR133-CTF at the lowest amount of DNA . The mutants show no significant difference from the WT.
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