Crystallographic studies of casein kinase I δ: Toward a structural understanding of auto-inhibition

K. L. Longenecker, Peter Roach, Thomas Hurley

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

A recombinant form of mammalian casein kinase I δ (CKIδ) containing the catalytic domain and an auto-inhibitory domain was expressed in Escherichia coli, purified and crystallized. X-ray data were collected to 2.4 Å resolution, and the crystals belong to space group C2221. Molecular replacement using the structure of the catalytic domain of CKIδ yielded strong electron density for residues in the model, but no interpretable density was found for the inhibitory domain. A conserved intermolecular contact suggests the formation of dimers which would inhibit the activity of this protein kinase.

Original languageEnglish
Pages (from-to)473-475
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume54
Issue number3
DOIs
StatePublished - 1998

Fingerprint

Casein Kinase I
Catalytic Domain
Dimers
Protein Kinases
Escherichia coli
Carrier concentration
X-Rays
Electrons
X rays
Crystals
Escherichia
dimers
proteins
crystals
x rays

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

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