Crystal structure of dopamine D1 receptor in complex with G protein and a non-catechol agonist
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Sun, Bingfa↗
Engineering topics
Kobilka, Brian K.
Publications and source records attributed to Kobilka, Brian K..
Structural insights into differences in G protein activation by family A and family B GPCRs
Family B heterotrimeric guanine nucleotide–binding protein (G protein)–coupled receptors (GPCRs) play important roles in carbohydrate metabolism. Recent structures of family B GPCR-G s protein complexes reveal a disruption in the α-helix of transmembrane segment 6 (TM6) not observed in family A GPCRs. To investigate the functional impact of this structural difference, we compared the structure and function of the glucagon receptor (GCGR; family B) with the β 2 adrenergic receptor (β 2 AR; family A). We determined the structure of the GCGR-G s complex by means of cryo–electron microscopy at 3.1-angstrom resolution. This structure shows the distinct break in TM6. Guanosine triphosphate (GTP) turnover, guanosine diphosphate release, GTP binding, and G protein dissociation studies revealed much slower rates for G protein activation by the GCGR compared with the β 2 AR. Fluorescence and double electron-electron resonance studies suggest that this difference is due to the inability of agonist alone to induce a detectable outward movement of the cytoplasmic end of TM6.
59 BASIC BIOLOGICAL SCIENCES↗
Structure and selectivity engineering of the M[subscript 1] muscarinic receptor toxin complex
Abstract not provided
Maeda, Shoji↗