A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1.

We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified subs...

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Publikašuvnnas:	Mol Cell Biol
Váldodahkkit:	Songyang, Z, Lu, K P, Kwon, Y T, Tsai, L H, Filhol, O, Cochet, C, Brickey, D A, Soderling, T R, Bartleson, C, Graves, D J, DeMaggio, A J, Hoekstra, M F, Blenis, J, Hunter, T, Cantley, L C
Materiálatiipa:	Artigo
Giella:	Inglês
Almmustuhtton:	Taylor & Francis 1996
Fáttát:	Research Article
Liŋkkat:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC231650/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8887677/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/mcb.16.11.6486
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A structural basis for substrate specificities of protein Ser/Thr kinases: primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1.

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