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

Kenton L. Longenecker, Peter J. Roach, Thomas D. Hurley

Research output: Contribution to journalArticle

22 Scopus citations

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

ASJC Scopus subject areas

  • Structural Biology

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