Elastic network model of allosteric regulation in protein kinase PDK1
- Single-subunit allostery in the kinetics of peptide phosphorylation by protein kinase A. Kuznetsov, Aleksei; Järv, Jaak // Proceedings of the Estonian Academy of Sciences;2008, Vol. 57 Issue 4, p247
Allosteric cooperativity between peptide and ATP binding sites on cAMP-dependent protein kinase catalytic subunit was studied kinetically for the reaction of phosphorylation of seven peptide substrates. The allosteric effect was quantified in terms of the interaction factor Î± by comparing...
- Synthesis and Biological Activity of Allosteric Modulators of GABAB Receptors. Part 4. Synthesis of Potentially Fluorescent Acridines and Conformationally Restricted N-(arylpropyl)-1-arylethylamines. Khalafy, Jabbar; Prager, Rolf H.; Puspawati, Ni Made // Turkish Journal of Chemistry;2008, Vol. 32 Issue 6, p755
A series of 8 new derivatives of fendiline was prepared for evaluation as allosteric modulators of GABAB receptors: 4 based on acridine and 4 with restricted distance between the 2 aryl moieties.
- Assembly of allosteric macromolecular switches: lessons from PKA. Taylor, Susan S.; Ilouz, Ronit; Zhang, Ping; Kornev, Alexandr P. // Nature Reviews Molecular Cell Biology;Oct2012, Vol. 13 Issue 10, p646
Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to...
- Engineered allosteric activation of kinases in living cells. Karginov, Andrei V.; Feng Ding; Kota, Pradeep; Dokholyan, Nikolay V.; Hahn, Klaus M. // Nature Biotechnology;Jul2010, Vol. 28 Issue 7, p743
Studies of cellular and tissue dynamics benefit greatly from tools that can control protein activity with specificity and precise timing in living systems. Here we describe an approach to confer allosteric regulation specifically on the catalytic activity of protein kinases. A highly conserved...
- Role of a Novel PH-Kinase Domain Interface in PKB/Akt Regulation: Structural Mechanism for Allosteric Inhibition. Calleja, Véronique; Laguerre, Michel; Parker, Peter J.; Larijani, Banafshé // PLoS Biology;Jan2009, Vol. 7 Issue 1, pe1000017
The mechanism of inhibition of the activity of the tumor-promoter protein kinase B operates via interactions across its functional domains.
- Double conjugation strategy for self-adjuvanting peptide vaccines. // Chemistry in Australia;May2016, p18
The article discusses a study on double conjugation strategy for self-adjuvanting peptide vaccines conducted by a team from Diamantina Institute and others that was published in the journal "Chemical Science" and established a synthetic pathway to conjugate peptide antigens and adjuvant moieties.
- Redox-sensitive inactivation of the phosphatase and tensin homolog deleted on chromosome 10 contribute to enhanced activation of phosphoinositide 3-kinase/serine/threonine protein kinase signaling in rostral ventrolateral medulla and neurogenic hypertension in spontaneously hypertensive rats. Chan, J. Y.; Chan, S. H. // Proceedings of the Physiological Society;2013, p616P
The activity of phosphoinositide 3-kinase (PI3K)/serine/threonine protein kinase (Akt) is enhanced under hypertension. The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a negative regulator of PI3K signaling, and its activity is redox-sensitive. In rostral ventrolateral...
- Biased binding of class IA phosphatidyl inositol 3-kinase subunits to inducible costimulator (CD278). Acosta, Yenny; Zafra, Maria; Ojeda, Gloria; Bernardone, Ilaria; Dianzani, Umberto; Portolés, Pilar; Rojo, Jose // Cellular & Molecular Life Sciences;Sep2011, Vol. 68 Issue 18, p3065
To better understand T lymphocyte costimulation by inducible costimulator (ICOS; H4; CD278), we analyzed proteins binding to ICOS peptides phosphorylated at the YMFM motif. Phosphorylated ICOS binds class IA phosphatidyl inositol 3-kinase (PI3-K) p85Î±, p50-55Î± and p85Î² regulatory...
- The conserved PI3â€²K/PTEN/Akt signaling pathway regulates both cell size and survival in Drosophila. Scanga, Sam E; Ruel, Laurent; Binari, Richard C; Snow, Brian; Stambolic, Vuk; Bouchard, Denis; Peters, Malte; Calvieri, Batista; Mak, Tak W; Woodgett, James R; Manoukian, Armen S // Oncogene;8/17/2000, Vol. 19 Issue 35, p3971
Akt (or PKB) is an oncogene involved in the regulation of cell survival. Akt is regulated by phosphatidylinositol 3-OH kinase (PI3â€²K) signaling and has shown to be hyperactivated through the loss of the PTEN tumor suppressor. In Drosophila, insulin signaling as studied using the Drosophila...