Crystal structure of casein kinase‐1, a phosphate‐directed protein kinase

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 differen...

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Bibliographic Details
Published in:The EMBO journal 1995-03, Vol.14 (5), p.1015-1023
Main Authors: Xu, R.M., Carmel, G., Sweet, R.M., Kuret, J., Cheng, X.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Amino Acid Sequence
Binding Sites
Casein Kinases
Crystallography, X-Ray
Models, Molecular
Molecular Sequence Data
Phosphorylation
Protein Conformation
Protein Kinases - chemistry
Protein Kinases - genetics
Protein Kinases - metabolism
Schizosaccharomyces - enzymology
schizosaccharomyces pombe
Sequence Alignment
Sequence Deletion
Substrate Specificity
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Description
Summary: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.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1995.tb07082.x