Author pages are created from data sourced from our academic publisher partnerships and public sources.
Share This Author
Structure of Mammalian AMPK and its regulation by ADP
It is shown that ADP binding to just one of the two exchangeable AXP (AMP/ADP/ATP) binding sites on the regulatory domain protects the enzyme from dephosphorylation, although it does not lead to allosteric activation.
Structural basis for AMP binding to mammalian AMP-activated protein kinase
The crystal structure of the regulatory fragment of mammalian AMPK in complexes with AMP and ATP is reported and suggests a mechanism for propagating AMP/ATP signalling whereby a phosphorylated residue from the α and/or β subunits binds to the γ subunit in the presence of AMP but not when ATP is bound.
Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma.
Ras activation of phosphoinositide 3-kinase (PI3K) is important for survival of transformed cells. We find that PI3Kgamma is strongly and directly activated by H-Ras G12V in vivo or by…
Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ
Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue
- K. Rittinger, P. Walker, J. Eccleston, S. Smerdon, S. Gamblin
- Chemistry, BiologyNature
- 16 October 1997
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.
H-NS oligomerization domain structure reveals the mechanism for high order self-association of the intact protein.
Role of guanine nucleotide-binding proteins--ras-family or trimeric proteins or both--in Ca2+ sensitization of smooth muscle.
It is concluded that p21rho may play a role in physiological Ca2+ sensitization as a cofactor with other messengers, rather than as a sole direct inhibitor of smooth muscle MLC20 phosphatase.
SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritima
The conserved arginine in rho-GTPase-activating protein is essential for efficient catalysis but not for complex formation with Rho.GDP and aluminum fluoride.
It is concluded that this arginine contributes half of the total reduction of activation energy of catalysis, and in the presence of aluminum fluoride, the R282A mutant RhoGAP binds almost as well as the wild type to Rho.GDP with aluminum fluoride.
Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
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.