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      The 2.0 A crystal structure of a heterotrimeric G protein.

      Nature

      Sequence Homology, Amino Acid, Amino Acid Sequence, chemistry, Recombinant Proteins, metabolism, Receptors, Cell Surface, Protein Processing, Post-Translational, Protein Conformation, Molecular Sequence Data, Models, Molecular, Humans, Guanosine Triphosphate, GTP-Binding Proteins, Escherichia coli, Crystallography, X-Ray, Cattle, Animals

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          Abstract

          The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor.

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          Journal
          10.1038/379311a0
          8552184

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