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