Structural determinants for activation of the α-subunit of a heterotrimeric G protein

@article{Lambright1994StructuralDF,
  title={Structural determinants for activation of the α-subunit of a heterotrimeric G protein},
  author={David G. Lambright and Joseph P Noel and Heidi E. Hamm and Paul B. Sigler},
  journal={Nature},
  year={1994},
  volume={369},
  pages={621-628}
}
  • David G. Lambright, Joseph P Noel, +1 author Paul B. Sigler
  • Published in Nature 1994
  • Biology
  • The 1.8 Å crystal structure of transducin α-GDP, when compared to that of the activated complex with GTP-γS, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein α-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily. 

    Create an AI-powered research feed to stay up to date with new papers like this posted to ArXiv

    Citations

    Publications citing this paper.
    SHOWING 1-10 OF 48 CITATIONS

    Insights into G protein structure, function, and regulation.

    VIEW 4 EXCERPTS
    CITES BACKGROUND

    Nucleotide-dependent movements of the kinesin motor domain predicted by simulated annealing.

    VIEW 9 EXCERPTS
    CITES BACKGROUND
    HIGHLY INFLUENCED

    Heterotrimeric C proteins: Organizers of transmembrane signals

    VIEW 4 EXCERPTS
    CITES BACKGROUND
    HIGHLY INFLUENCED