Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: role in catalysis, P-site specificity, and interaction with inhibitors.
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Structural and functional diversity of the microbial kinomeStructure of the human protein kinase MPSK1 reveals an atypical activation loop architectureCrystal Structures of the p21-Activated Kinases PAK4, PAK5, and PAK6 Reveal Catalytic Domain Plasticity of Active Group II PAKsThe Crystal Structures of Substrate and Nucleotide Complexes of Enterococcus faecium Aminoglycoside-2''-Phosphotransferase-IIa [APH(2'')-IIa] Provide Insights into Substrate Selectivity in the APH(2'') SubfamilyAminoglycoside 2′′-Phosphotransferase IIIa (APH(2′′)-IIIa) Prefers GTP over ATPInsights into the Phosphoryl Transfer Catalyzed by cAMP-Dependent Protein Kinase: An X-ray Crystallographic Study of Complexes with Various Metals and Peptide Substrate SP20Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor SpecificityMetal-Free cAMP-Dependent Protein Kinase Can Catalyze Phosphoryl TransferStructure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6′)-Ie-APH(2′′)-IaSite-directed mutagenesis of the glycine-rich loop of death associated protein kinase (DAPK) identifies it as a key structure for catalytic activity.Fluorescent biosensors for high throughput screening of protein kinase inhibitors.Allosteric cooperativity in protein kinase A.Release of ADP from the catalytic subunit of protein kinase A: a molecular dynamics simulation study.The mechanism of inhibition of the cyclin-dependent kinase-2 as revealed by the molecular dynamics study on the complex CDK2 with the peptide substrate HHASPRKActivation and inhibition of cyclin-dependent kinase-2 by phosphorylation; a molecular dynamics study reveals the functional importance of the glycine-rich loop.Solution NMR Spectroscopy for the Study of Enzyme Allostery.Ca(2+)/calmodulin-dependent protein kinases.Biochemical mechanisms of resistance to small-molecule protein kinase inhibitors.Characterization of the mechanisms controlling Greatwall activity.Saccharomyces cerevisiae Env7 is a novel serine/threonine kinase 16-related protein kinase and negatively regulates organelle fusion at the lysosomal vacuole.E pluribus unum? The main protein kinase A catalytic subunit (PRKACA), a likely oncogene, and cortisol-producing tumors.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.A conserved salt bridge in the G loop of multiple protein kinases is important for catalysis and for in vivo Lyn function.Investigation of invariant serine/threonine residues in mevalonate kinase. Tests of the functional significance of a proposed substrate binding motif and a site implicated in human inherited disease.Structural basis for peptide binding in protein kinase A. Role of glutamic acid 203 and tyrosine 204 in the peptide-positioning loop.Different mechanisms of CDK5 and CDK2 activation as revealed by CDK5/p25 and CDK2/cyclin A dynamics.Activating PRKACB somatic mutation in cortisol-producing adenomas.Mechanism of kinase inactivation and nonbinding of FRATide to GSK3β due to K85M mutation: molecular dynamics simulation and normal mode analysis.A QM/MM study of the associative mechanism for the phosphorylation reaction catalyzed by protein kinase A and its D166A mutant.The effect of Li+ on GSK-3 inhibition: molecular dynamics simulation.
P2860
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P2860
Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: role in catalysis, P-site specificity, and interaction with inhibitors.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
@zh
2000年论文
@zh-cn
name
Serine-53 at the tip of the gl ...... d interaction with inhibitors.
@en
type
label
Serine-53 at the tip of the gl ...... d interaction with inhibitors.
@en
prefLabel
Serine-53 at the tip of the gl ...... d interaction with inhibitors.
@en
P2093
P356
P1433
P1476
Serine-53 at the tip of the gl ...... d interaction with inhibitors.
@en
P2093
P304
P356
10.1021/BI992800W
P407
P577
2000-07-01T00:00:00Z