How converging fingers keep GTP in line

@article{Bourne1997HowCF,
  title={How converging fingers keep GTP in line},
  author={Henry R. Bourne},
  journal={Nature},
  year={1997},
  volume={389},
  pages={674-674}
}
1 Citations
Novel intermediate of Rac GTPase activation by guanine nucleotide exchange factor.
TLDR
TrioN, a Dbl family GEF, activates Rac1 by facilitating GTP binding to, as well as stimulating GDP dissociation from, Rac1, and it is proposed that the Rac GEF reaction may proceed by competitive displacement of bound GDP by GTP through a transient intermediate of GEF-[GTP-Rac-GDP]. Expand

References

SHOWING 1-4 OF 4 REFERENCES
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
TLDR
It is proposed that rhoGAP adopts a different conformation during the catalytic cycle which enables it to stabilize the transition state of the GTP-hydrolysis reaction. Expand
Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
TLDR
The crystal structure of RhoA and rhoGAP complexed with the transition-state analogue GDP is reported and it is proposed that this residue acts to stabilize the transition state of the GTPase reaction. Expand
The GTPase superfamily: conserved structure and molecular mechanism
GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases—crystal structures, biochemical properties, or results ofExpand
GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumours
A subset of growth hormone-secreting human pituitary tumours carries somatic mutations that inhibit GTPase activity of a G protein α chain, αs. The resulting activation of adenylyl cyclase bypassesExpand