1CKI

RECOMBINANT CASEIN KINASE I DELTA TRUNCATION MUTANT CONTAINING RESIDUES 1-317

1CKI の概要

• エントリーDOI: 10.2210/pdb1cki/pdb
• 分子名称: CASEIN KINASE I DELTA (2 entities in total)
• 機能のキーワード: protein kinase, phosphotransferase
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm (By similarity): Q06486
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73991.06

構造登録者

Longenecker, K.L.,Roach, P.J.,Hurley, T.D. (登録日: 1995-08-25, 公開日: 1995-12-07, 最終更新日: 2024-02-07)

主引用文献

Longenecker, K.L.,Roach, P.J.,Hurley, T.D.
Three-dimensional structure of mammalian casein kinase I: molecular basis for phosphate recognition.
J.Mol.Biol., 257:618-631, 1996

PubMed Abstract: The three-dimensional structure for the catalytic region of the mammalian protein kinase, casein kinase I delta (CKI delta), has been solved by X-ray crystallography to a resolution of 2.3 A. A truncation mutant of CKI delta lacking the C-terminal autoinhibitory region was expressed in Escherichia coli, purified, and crystallized. The structure was solved by molecular replacement using the crystal structure of the catalytic domain of a CKI homolog from Schizosaccharomyces pombe, Cki1. A tungstate derivative confirmed the initial molecular replacement solution and identified an anion binding site which may contribute to the unique substrate specificity of CKI. Like other protein kinases, the catalytic domain of CKI is composed of two lobes with a cleft between them for binding ATP. Comparison of the mammalian and yeast CKI structures suggests that a rotation of the N-terminal domain occurs upon ATP binding. This domain motion is similar, but not identical, to that observed in cAMP-dependent protein kinase upon binding ATP. Although Cki1 has many similarities to CKI delta over the catalytic domain, these two forms of CKI likely perform different functions in vivo. Relating the primary sequences of other CKI enzymes to the three-dimensional architecture of CKI delta reveals a catalytic face that is especially conserved among the subset of CKI family members associated with the regulation of DNA repair.

PubMed: 8648628
DOI: 10.1006/jmbi.1996.0189

実験手法

X-RAY DIFFRACTION (2.3 Å)