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10.1074/jbc.M116.724310 http://scihub22266oqcxt.onion/10.1074/jbc.M116.724310 C5034064!5034064 !27514745     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=27514745 &cmd=llinks): Failed to open stream: HTTP request failed! 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Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1) |pdf=|usr=}}{{27514745 }} gab.com Text Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1) JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27514745 #FOAvip Apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5), a member of the mitogen-activated protein kinase kinase kinase (MAP3K) family, regulates diverse physiological processes. The activity of ASK1 is triggered by various stress stimuli and is involved in the pathogenesis of cancer, neurodegeneration, inflammation, and diabetes. ASK1 forms a high molecular mass complex whose activity is, under non-stress conditions, suppressed through interaction with thioredoxin and the scaffolding protein 14-3-3. The 14-3-3 protein binds to the phosphorylated Ser-966 motif downstream of the ASK1 kinase domain. The role of 14-3-3 in the inhibition of ASK1 has yet to be elucidated. In this study we performed structural analysis of the complex between the ASK1 kinase domain phosphorylated at Ser-966 (pASK1-CD) and the 14-3-3? protein. Small angle x-ray scattering (SAXS) measurements and chemical cross-linking revealed that the pASK1-CD·14-3-3? complex is dynamic and conformationally heterogeneous. In addition, structural analysis coupled with the results of phosphorus NMR and time-resolved tryptophan fluorescence measurements suggest that 14-3-3? interacts with the kinase domain of ASK1 in close proximity to its active site, thus indicating this interaction might block its accessibility and/or affect its conformation. Twit Text FOAVip Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1) ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=27514745 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27514745 #FOAvip English Wikipedia <ref>{{Cite pmid|27514745 }}</ref> Structural Insight into the 14-3-3 Protein-dependent Inhibition of Protein Kinase ASK1 (Apoptosis Signal-regulating kinase 1) #MMPMID27514745 Petrvalska O ; Kosek D ; Kukacka Z ; Tosner Z ; Man P ; Vecer J ; Herman P ; Obsilova V ; Obsil T J Biol Chem 2016[Sep]; 291 (39 ): 20753-65 PMID27514745 show ga Apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5), a member of the mitogen-activated protein kinase kinase kinase (MAP3K) family, regulates diverse physiological processes. The activity of ASK1 is triggered by various stress stimuli and is involved in the pathogenesis of cancer, neurodegeneration, inflammation, and diabetes. ASK1 forms a high molecular mass complex whose activity is, under non-stress conditions, suppressed through interaction with thioredoxin and the scaffolding protein 14-3-3. The 14-3-3 protein binds to the phosphorylated Ser-966 motif downstream of the ASK1 kinase domain. The role of 14-3-3 in the inhibition of ASK1 has yet to be elucidated. In this study we performed structural analysis of the complex between the ASK1 kinase domain phosphorylated at Ser-966 (pASK1-CD) and the 14-3-3? protein. Small angle x-ray scattering (SAXS) measurements and chemical cross-linking revealed that the pASK1-CD·14-3-3? complex is dynamic and conformationally heterogeneous. In addition, structural analysis coupled with the results of phosphorus NMR and time-resolved tryptophan fluorescence measurements suggest that 14-3-3? interacts with the kinase domain of ASK1 in close proximity to its active site, thus indicating this interaction might block its accessibility and/or affect its conformation. |14-3-3 Proteins/*chemistry/genetics/metabolism [MESH] |Catalytic Domain [MESH] |Humans [MESH] |MAP Kinase Kinase Kinase 5/*antagonists & inhibitors/*chemistry/genetics/metabolism [MESH] |Nuclear Magnetic Resonance, Biomolecular [MESH] |Phosphorylation [MESH] |Scattering, Small Angle [MESH]Structural Insight into the 14-3-3 Protein-dependent Inhibition of Pro(epmc).pdf DeepDyve Pubget Overpricing