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

Lambright DG, Noel JP, Hamm HE, Sigler PB
Nature. 1994 369 (6482): 621-8

PMID: 8208289 · DOI:10.1038/369621a0

The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-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.

MeSH Terms (17)

Amino Acid Sequence Animals Cattle Computer Graphics Crystallography, X-Ray Guanosine Diphosphate Guanosine Triphosphate Humans Mice Molecular Sequence Data Peptide Elongation Factor Tu Peptide Fragments Protein Conformation Proto-Oncogene Proteins p21(ras) Rod Cell Outer Segment Structure-Activity Relationship Transducin

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