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Crystal structure of casein kinase‐1, a phosphate‐directed protein kinase.
Author(s) -
Xu R.M.,
Carmel G.,
Sweet R.M.,
Kuret J.,
Cheng X.
Publication year - 1995
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1995.tb07082.x
Subject(s) - spring (device) , structural biology , biology , library science , physics , biochemistry , computer science , thermodynamics
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.