BETA 1 ADRENERGIC RECEPTOR;
DIMER;
G PROTEIN COUPLED RECEPTOR;
GUANINE NUCLEOTIDE BINDING PROTEIN;
HOMODIMER;
MEMBRANE PROTEIN;
MU OPIATE RECEPTOR;
OLIGOMER;
TETRAMER;
PROTEIN BINDING;
COMPLEX FORMATION;
CONFORMATIONAL TRANSITION;
CRYSTAL STRUCTURE;
HUMAN;
INTRACELLULAR SIGNALING;
OLIGOMERIZATION;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN DOMAIN;
PROTEIN FUNCTION;
PROTEIN PROTEIN INTERACTION;
PROTEIN STRUCTURE;
SHORT SURVEY;
STRUCTURE ACTIVITY RELATION;
ANIMAL;
CHEMISTRY;
METABOLISM;
ANIMALS;
GTP-BINDING PROTEINS;
HUMANS;
PROTEIN BINDING;
PROTEIN CONFORMATION;
RECEPTORS, G-PROTEIN-COUPLED;
Modeling of G protein-coupled receptors using crystal structures: from monomers to signaling complexes
Gonzalez A., et al. Modeling of G protein-coupled receptors using crystal structures: from monomers to signaling complexes. Adv. Exp. Med. Biol. 2014, 796:15-33.
Structural flexibility of the G α s α-helical domain in the β2-adrenoceptor Gs complex
Westfield G.H., et al. Structural flexibility of the G α s α-helical domain in the β2-adrenoceptor Gs complex. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:16086-16091.