DOI . ORG {
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We began analyzing https://link.springer.com/article/10.1007/BF02737887, but it redirected us to https://link.springer.com/article/10.1007/BF02737887. The analysis below is for the second page.
Title[redir]:
Calcineurin | Cell Biochemistry and Biophysics
Description:
Calcineurin is a serine-threonine specific Ca2+-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506. Both drugs form complexes with abundant intracellular binding proteins, cyclosporin A with cyclophilin A and FK506 with FKBP 12, which bind to and inhibit calcineurin. The X-ray structure of an FKPB12-FK506-calcineurin AB ternary complex reveals that FKBP12-FK506 binds in a hydophobic groove between the calcineurin A catalytic and the regulatory B subunit, in accord with biochemical and genetic studies on inhibitor action. Calcineurin plays a key role in regulating the transcription factor NF-AT during T-cell activation, and in mediating responses of microorganisms to cation stress. These findings highlight the potential of yeast genetic studies to define novel drug targets and elucidate conserved elements of signal transduction cascades.
Title[redir]:
Calcineurin | Cell Biochemistry and Biophysics
Description:
Calcineurin is a serine-threonine specific Ca2+-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506. Both drugs form complexes with abundant intracellular binding proteins, cyclosporin A with cyclophilin A and FK506 with FKBP 12, which bind to and inhibit calcineurin. The X-ray structure of an FKPB12-FK506-calcineurin AB ternary complex reveals that FKBP12-FK506 binds in a hydophobic groove between the calcineurin A catalytic and the regulatory B subunit, in accord with biochemical and genetic studies on inhibitor action. Calcineurin plays a key role in regulating the transcription factor NF-AT during T-cell activation, and in mediating responses of microorganisms to cation stress. These findings highlight the potential of yeast genetic studies to define novel drug targets and elucidate conserved elements of signal transduction cascades.
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Keywords {π}
google, scholar, cas, pubmed, calcineurin, protein, biol, chem, phosphatase, cell, sci, usa, natl, acad, klee, heitman, yeast, cyclosporin, subunit, factor, activation, gene, article, structure, hemenway, binding, human, kincaid, brain, calmodulindependent, regulation, function, inhibition, transcription, identification, cerevisiae, calcium, activity, access, cardenas, cohen, cyclic, phosphatases, calmodulin, perrino, soderling, nuclear, cells, essential, target,
Topics {βοΈ}
peptidyl-prolyl cis-trans isomerase ca2+/calmodulin-stimulated protein phosphatase ca2+-calmodulin-dependent protein kinase ca2+/calmodulin-dependent phosphoprotein phosphatase immunophilin-immunosuppressant fkbp12-fk506 complex cis-trans peptidyl-prolylisomerase human fkbp12-fk506-calcineurin complex month download article/chapter peptidyl-prolylcis-trans isomerase calmodulin-dependent protein phosphatase camp-dependent protein kinase endogenous ca2+-dependent phosphatase ca2+-calmodulin promotes survival cyclic nucleotide phosphodiesterase immunosuppressant-immunophilin complex docking hippocampal long-term depression sodium- extrusion genepmr2/ena1 ca2+/calmodulin-regulated phosphatases 3-Ξ²-d-glucan synthase calmodulin-regulated phosphoprotein phosphatase calcineurin inhibits vcx1-dependent immunophilin-ligand complexes correlates yeast cls2p/csg2p localized nh2-terminal blocking group stimulus-secretion coupling revealed ca2+-activated cell death human fk506-binding protein transcription factor nf-at4 related subjects calmodulin-dependent phosphatase lymphocyte dna-binding protein calcium insaccharomyces cerevisiae fk506-sensitive yeast strains bovine brain residues cyclosporin a-treated human mammalian na+/ca2+ exchangers calcineurin/inhibitor-1 phosphatase cascade pheromone-induced growth arrest calmodulin-binding proteins molecular mechanisms protein phosphatase 2b modulator binding protein calmodulin-dependent activation calmodulin-binding protein full article pdf drug-immunophinlin complexes t-lymphocyte activation nitric oxide synthase Ξ±-factor arrest privacy choices/manage cookies
Questions {β}
- (1991) Can calmodulin function without binding calcium?
Schema {πΊοΈ}
WebPage:
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headline:Calcineurin
description:Calcineurin is a serine-threonine specific Ca2+-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506. Both drugs form complexes with abundant intracellular binding proteins, cyclosporin A with cyclophilin A and FK506 with FKBP 12, which bind to and inhibit calcineurin. The X-ray structure of an FKPB12-FK506-calcineurin AB ternary complex reveals that FKBP12-FK506 binds in a hydophobic groove between the calcineurin A catalytic and the regulatory B subunit, in accord with biochemical and genetic studies on inhibitor action. Calcineurin plays a key role in regulating the transcription factor NF-AT during T-cell activation, and in mediating responses of microorganisms to cation stress. These findings highlight the potential of yeast genetic studies to define novel drug targets and elucidate conserved elements of signal transduction cascades.
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T-cell activation
yeast genetics
drug targets
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description:Calcineurin is a serine-threonine specific Ca2+-calmodulin-activated protein phosphatase that is conserved from yeast to humans. Remarkably, this enzyme is the common target for two novel and structurally unrelated immunosuppressive antifungal drugs, cyclosporin A and FK506. Both drugs form complexes with abundant intracellular binding proteins, cyclosporin A with cyclophilin A and FK506 with FKBP 12, which bind to and inhibit calcineurin. The X-ray structure of an FKPB12-FK506-calcineurin AB ternary complex reveals that FKBP12-FK506 binds in a hydophobic groove between the calcineurin A catalytic and the regulatory B subunit, in accord with biochemical and genetic studies on inhibitor action. Calcineurin plays a key role in regulating the transcription factor NF-AT during T-cell activation, and in mediating responses of microorganisms to cation stress. These findings highlight the potential of yeast genetic studies to define novel drug targets and elucidate conserved elements of signal transduction cascades.
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