Crystal Structure of Glycogen Synthase Kinase 3β Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition
@article{Dajani2001CrystalSO, title={Crystal Structure of Glycogen Synthase Kinase 3$\beta$ Structural Basis for Phosphate-Primed Substrate Specificity and Autoinhibition}, author={Rana Dajani and Elizabeth Fraser and Stephen Mark Roe and Neville Young and Valerie M. Good and Trevor C. Dale and Laurence H. Pearl}, journal={Cell}, year={2001}, volume={105}, pages={721-732} }
609 Citations
Allosteric Regulation of Glycogen Synthase Kinase 3β: A Theoretical Study†
- Biology, ChemistryBiochemistry
- 2010
It is found that GSK-3β autophosphorylation at residue Tyr216 results in widening of the catalytic groove, thereby facilitating substrate access and it is speculated that this stabilization could enhanceThe catalytic activity of the kinase.
Identification of Novel Glycogen Synthase Kinase-3β Substrate-interacting Residues Suggests a Common Mechanism for Substrate Recognition*
- BiologyJournal of Biological Chemistry
- 2006
This work combined in silico modeling with mutagenesis and biological studies to identify GSK-3-substrate interaction sites located within its binding cleft, and identified Phe67, Gln89, and Asn95 of G SK-3β as putative binding sites interacting with the CREB phosphorylation motif.
Structural basis of GSK-3 inhibition by N-terminal phosphorylation and by the Wnt receptor LRP6
- BiologyeLife
- 2014
A conserved loop unique to GSK-3 undergoes a dramatic conformational change that clamps the bound pseudo-substrate peptides, and reveals the mechanism of primed substrate recognition, which rationalize target sequence preferences and suggest avenues for the design of inhibitors selective for a subset of pathways regulated by GK-3.
A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation.
- Biology, ChemistryMolecular cell
- 2001
The Structure of Phosphorylated GSK-3β Complexed with a Peptide, FRATtide, that Inhibits β-Catenin Phosphorylation
- Biology, Chemistry
- 2001
New insights into the autoinhibition mechanism of glycogen synthase kinase-3beta.
- Biology, ChemistryJournal of molecular biology
- 2008
Structural insight into nucleotide recognition in tau-protein kinase I/glycogen synthase kinase 3 beta.
- Biology, ChemistryActa crystallographica. Section D, Biological crystallography
- 2004
Binary complex structures of full-length TPK I/GSK3 beta with the ATP analogues ADP and AMPPNP solved by the X-ray diffraction method at 2.1 and 1.8 A resolution are reported.
New Insights into the Autoinhibition Mechanism of Glycogen Synthase Kinase-3 β
- Biology, Chemistry
- 2008
This study supports a model of GSK-3–pseudosubstrate autoregulation that involves phosphorylated Ser9, Arg4, and Arg6 within the N-terminus and identified the specific contact sites within the catalytic core.
Structural basis for the complete loss of GSK3β catalytic activity due to R96 mutation investigated by molecular dynamics study
- Chemistry, BiologyProteins
- 2009
Experimental mutagenesis proved that the residue arginine at amino acid 96 mutations to lysine or alanine selectively abolish activity on the substrates involved in glycogen synthesis signaling pathway, and the allosteric mechanisms for distorted ATP were proposed.
Role of T-loop Phosphorylation in PDK1 Activation, Stability, and Substrate Binding*
- Biology, ChemistryJournal of Biological Chemistry
- 2005
It is demonstrated by mutational analysis that interactions between the phosphorylated Ser-241 and the αC-helix are not required for PDK1 activity or substrate binding through the HM-pocket but are necessary forPDK1 to be activated or stabilized by a peptide that binds to this site.
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