Identification of intramolecular interactions in adrenergic receptors.
Adrenergic receptors are representative of a large family of plasma membrane receptors that interact with G proteins during the process of transmembrane signal transduction. G protein-coupled receptors have a primary structure that is homologous to bacteriorhodopsin and are proposed to have a similar three-dimensional structure; however, it has not yet been possible to examine this hypothesis experimentally. We have used a novel mutagenesis approach to identify intramolecular interactions. Our results indicate that specific amino acids in the seventh hydrophobic segment of alpha 2 and beta 2 adrenergic receptors lie adjacent to the first hydrophobic segment. These studies provide the first experimental evidence defining spatial relationships that exist in the three-dimensional structure of adrenergic receptors.
Suryanarayana
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S
Howard Hughes Medical Institute, Stanford University Medical Center, California 94305.
von Zastrow
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M
Kobilka
B K
BK
D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology; D016297:Mutagenesis, Site-Directed; D011942:Receptors, Adrenergic, alpha / Q000737:chemistry / Q000502:physiology*; D011943:Receptors, Adrenergic, beta / Q000737:chemistry / Q000502:physiology*; D011993:Recombinant Fusion Proteins; D012995:Solubility; D013329:Structure-Activity Relationship
D046911:Macromolecular Substances; D008565:Membrane Proteins; D011942:Receptors, Adrenergic, alpha; D011943:Receptors, Adrenergic, beta; D011993:Recombinant Fusion Proteins