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

EMBO J. 1995 Mar 1;14(5):1015-23.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 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
  • Sequence Alignment
  • Sequence Deletion
  • Substrate Specificity

Substances

  • Adenosine Triphosphate
  • Protein Kinases
  • Casein Kinases