RETRACTED: Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gβ1γ2 (Retracted article. See vol. 19, pg. 1200, 2011)

A critical role of the G beta gamma dimer in heterotrimeric G-protein signaling is to facilitate the engagement and activation of the G alpha subunit by cell-surface G-protein-coupled receptors. However, high-resolution structural information of the connectivity between receptor and the G beta gamma dimer has not previously been available. Here, we describe the structural determinants of G beta(1)gamma(2) in complex with a C-terminal region of the parathyroid hormone receptor-1 (PTH1R) as obtained by X-ray crystallography. The structure reveals that several critical residues within PTH1R contact only G beta residues located within the outer edge of WD1- and WD7-repeat segments of the G beta toroid structure. These regions encompass a predicted membrane-facing region of G beta thought to be oriented in a fashion that is accessible to the membrane-spanning receptor. Mutation of key receptor contact residues on G beta(1) leads to a selective loss of function in receptor/heterotrimer coupling while preserving G beta(1)gamma(2) activation of the effector phospholipase-C beta.