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. 1995 Mar 1;14(5):1015–1023. doi: 10.1002/j.1460-2075.1995.tb07082.x

Crystal structure of casein kinase-1, a phosphate-directed protein kinase.

R M Xu 1, G Carmel 1, R M Sweet 1, J Kuret 1, X Cheng 1
PMCID: PMC398173  PMID: 7889932

Abstract

The structure of a truncated variant of casein kinase-1 from Schizosaccharomyces pombe, has been determined in complex with MgATP at 2.0 A resolution. The model resembles the 'closed', ATP-bound conformations of the cyclin-dependent kinase 2 and the cAMP-dependent protein kinase, with clear differences in the structure of surface loops that impart unique features to casein kinase-1. The structure is of unphosphorylated, active conformation of casein kinase-1 and the peptide-binding site is fully accessible to substrate.

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